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Identification
- Summary
L-Glutamine is an amino acid commonly found as a component in total parenteral nutrition.
- Brand Names
- Endari
- Generic Name
- L-Glutamine
- DrugBank Accession Number
- DB00130
- Background
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from glutamic acid and ammonia. It is the principal carrier of nitrogen in the body and is an important energy source for many cells. An oral formulation of L-glutamine was approved by the FDA in July 2017 for use in sickle cell disease 5. This oral formulation is marketed under the tradename Endari by Emmaus Medical.
- Type
- Small Molecule
- Groups
- Approved, Investigational, Nutraceutical
- Structure
Structure for L-Glutamine (DB00130)
- Weight
- Average: 146.1445
Monoisotopic: 146.069142196 - Chemical Formula
- C5H10N2O3
- Synonyms
- (2S)-2-amino-4-carbamoylbutanoic acid
- (2S)-2,5-diamino-5-oxopentanoic acid
- (S)-2,5-diamino-5-oxopentanoic acid
- Glutamic acid 5-amide
- Glutamic acid amide
- Glutamina
- Glutamine
- L-(+)-glutamine
- L-2-aminoglutaramic acid
- L-glutamic acid γ-amide
- L-Glutamin
- L-Glutamine
- L-Glutaminsäure-5-amid
- Levoglutamide
- Q
- External IDs
- Fema no. 3684
- NSC-27421
Pharmacology
- Indication
Used for nutritional supplementation, also for treating dietary shortage or imbalance.
Used to reduce the acute complications of sickle cell disease in adult and pediatric patients 5 years of age and older Label.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Used in combination to manage Osteoporosis Combination Product in combination with: Calcium citrate (DB11093), Calcium gluconate (DB11126) •••••••••••• Treatment of Acute complications of sickle cell disease •••••••••••• - Contraindications & Blackbox Warnings
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Like other amino acids, glutamine is biochemically important as a constituent of proteins. Glutamine is also crucial in nitrogen metabolism. Ammonia (formed by nitrogen fixation) is assimilated into organic compounds by converting glutamic acid to glutamine. The enzyme which accomplishes this is called glutamine synthetase. Glutamine can then be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, purines, and pyrimidines.
L-glutamine improves nicotinamide adenine dinucleotide (NAD) redox potential Label.
- Mechanism of action
Supplemental L-glutamine's possible immunomodulatory role may be accounted for in a number of ways. L-glutamine appears to play a major role in protecting the integrity of the gastrointestinal tract and, in particular, the large intestine. During catabolic states, the integrity of the intestinal mucosa may be compromised with consequent increased intestinal permeability and translocation of Gram-negative bacteria from the large intestine into the body. The demand for L-glutamine by the intestine, as well as by cells such as lymphocytes, appears to be much greater than that supplied by skeletal muscle, the major storage tissue for L-glutamine. L-glutamine is the preferred respiratory fuel for enterocytes, colonocytes and lymphocytes. Therefore, supplying supplemental L-glutamine under these conditions may do a number of things. For one, it may reverse the catabolic state by sparing skeletal muscle L-glutamine. It also may inhibit translocation of Gram-negative bacteria from the large intestine. L-glutamine helps maintain secretory IgA, which functions primarily by preventing the attachment of bacteria to mucosal cells. L-glutamine appears to be required to support the proliferation of mitogen-stimulated lymphocytes, as well as the production of interleukin-2 (IL-2) and interferon-gamma (IFN-gamma). It is also required for the maintenance of lymphokine-activated killer cells (LAK). L-glutamine can enhance phagocytosis by neutrophils and monocytes. It can lead to an increased synthesis of glutathione in the intestine, which may also play a role in maintaining the integrity of the intestinal mucosa by ameliorating oxidative stress. The exact mechanism of the possible immunomodulatory action of supplemental L-glutamine, however, remains unclear. It is conceivable that the major effect of L-glutamine occurs at the level of the intestine. Perhaps enteral L-glutamine acts directly on intestine-associated lymphoid tissue and stimulates overall immune function by that mechanism, without passing beyond the splanchnic bed.
The exact mechanism of L-glutamine's effect on NAD redox potential is unknown but is thought to involve increased amounts of reduced glutathione made available by glutamine supplementation Label. This improvement in redox potential reduces the amount of oxidative damage which sickle red blood cells are more susceptible to. The reduction in cellular damage is thought to reduce chronic hemolysis and vaso-occlusive events.
Target Actions Organism UCTP synthase 1 antagonistsubstrateHumans UAmidophosphoribosyltransferase substrateHumans UGlutamine synthetase product ofHumans - Absorption
Absorption is efficient and occurs by an active transport mechanism. Tmax is 30 minutes after a single dose Label. Absorption kinetics following multiple doses has not yet been determined.
- Volume of distribution
Volume of distribution is 200 mL/kg after intravenous bolus dose Label.
- Protein binding
Not Available
- Metabolism
Exogenous L-glutamine likely follows the same metabolic pathways as endogenous L-glutamine which is involved in the formation of glutamate, proteins, nucleotides, and amino acid sugars Label.
Hover over products below to view reaction partners
- Route of elimination
Primarily eliminated by metabolism Label. While L-glutamine is filtered though the glomerulus, nearly all is reabsorbed by renal tubules.
- Half-life
The half life of elimination is 1 h Label.
- Clearance
Not Available
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Doses of L-glutamine up to 21 grams daily appear to be well tolerated. Reported adverse reactions are mainly gastrointestinal and not common. They include constipation and bloating. There is one older report of two hypomanic patients whose manic symptoms were exacerbated following the use of 2 to 4 grams daily of L-glutamine. The symptoms resolved when the L-glutamine was stopped. These patients were not rechallenged, nor are there any other reports of this nature.
The most common adverse effects observed in clinical trials of Endari were constipation (21%), nausea (19%), headache (18%), abdominal pain (17%), cough (16%), extremity pain (13%), back pain (12%), and chest pain (12%) Label.
- Pathways
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareLactulose The therapeutic efficacy of Lactulose can be decreased when used in combination with L-Glutamine. - Food Interactions
- Take with food. Endari (L-glutamine) oral powder should be mixed with 8oz of water or 4-6 oz of food at room temperature or colder, then consumed.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Product Ingredients
Ingredient UNII CAS InChI Key Glutamine sodium IA7707HOQ8 73477-31-3 YWOPZILGDZKFFC-DFWYDOINSA-M - International/Other Brands
- Earthlink Science Glutamine Chews Chocolate (Amerifit) / Glutamine Express (Genetic Evolutionary Nutrition) / Glutamine Fuel Mega (Twinlab) / Glutamine Fuel Powder (Twinlab) / L-Glutamine Power (Champion Nutrition)
- Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Endari Powder, for solution 5 g/1 Oral Emmaus Medical, Inc. 2017-07-07 Not applicable US 
NutreStore Powder, for solution 5 g/1 Oral Emmaus Medical, Inc. 2008-06-04 2018-08-31 US - Generic Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image L-Glutamine Powder, for solution 5 g/1 Oral ANI Pharmaceuticals, Inc. 2024-07-11 Not applicable US - Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image GNC L-Glutamine 1000 Tablet Tablet 1000 mg Oral GNC LIVEWELL MALAYSIA SDN. BHD. 2020-09-08 Not applicable Malaysia 
- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image MEMOVIT B12 L-Glutamine (60 mg) + Cyanocobalamin (500 mcg/10g) + Dexfosfoserine (40 mg/10g) Syrup Oral Aescul API Us Farmaceutici Srl 2018-06-05 Not applicable Italy 
MEMOVIT B12 L-Glutamine (60 mg) + Cyanocobalamin (500 mcg/10g) + Dexfosfoserine (40 mg/10g) Syrup Oral Aescul API Us Farmaceutici Srl 2014-07-08 Not applicable Italy - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image ABOUND PORTAKAL AROMALI TOZ 24 GR 30 POSET L-Glutamine (7 g/1) + Arginine (7 g/1) Powder Oral ABBOTT LABORATUARLARI İTHALAT İHRACAT VE TİC. LTD. ŞTİ. 2013-01-29 2024-01-23 Turkey 
NUTRIMED GLUTAMIN 100 GR (20X5) L-Glutamine (100 gr) Powder Oral NUTRİMEDİCA GIDA SAN. VE TİC. LTD. ŞTİ. 2013-03-12 Not applicable Turkey NUTRIMEDICA GLUTAMIN 100 GR (20X5) L-Glutamine (100 gr) Powder Oral NUTRİMEDİCA GIDA SAN. VE TİC. LTD. ŞTİ. 2019-11-26 Not applicable Turkey
Categories
- ATC Codes
- A16AA03 — Glutamine
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
- Kingdom
- Organic compounds
- Super Class
- Organic acids and derivatives
- Class
- Carboxylic acids and derivatives
- Sub Class
- Amino acids, peptides, and analogues
- Direct Parent
- L-alpha-amino acids
- Alternative Parents
- Fatty acids and conjugates / Amino acids / Monocarboxylic acids and derivatives / Carboxylic acids / Carboximidic acids / Organopnictogen compounds / Organic oxides / Monoalkylamines / Hydrocarbon derivatives / Carbonyl compounds
- Substituents
- Aliphatic acyclic compound / Amine / Amino acid / Carbonyl group / Carboximidic acid / Carboximidic acid derivative / Carboxylic acid / Fatty acid / Hydrocarbon derivative / L-alpha-amino acid
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- proteinogenic amino acid, L-alpha-amino acid, glutamine, glutamine family amino acid (CHEBI:18050) / Common amino acids (C00064)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- 0RH81L854J
- CAS number
- 56-85-9
- InChI Key
- ZDXPYRJPNDTMRX-VKHMYHEASA-N
- InChI
- InChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
- IUPAC Name
- (2S)-2-amino-4-carbamoylbutanoic acid
- SMILES
- N[C@@H](CCC(N)=O)C(O)=O
References
- Synthesis Reference
Stephen Paul, "Novel preparation of fiber, L-glutamine and a soy derivative for the purpose of enhancement of isoflavone bioavailability." U.S. Patent US20020076455, issued June 20, 2002.
US20020076455- General References
- Boza JJ, Dangin M, Moennoz D, Montigon F, Vuichoud J, Jarret A, Pouteau E, Gremaud G, Oguey-Araymon S, Courtois D, Woupeyi A, Finot PA, Ballevre O: Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers. Am J Physiol Gastrointest Liver Physiol. 2001 Jul;281(1):G267-74. [Article]
- McAnena OJ, Moore FA, Moore EE, Jones TN, Parsons P: Selective uptake of glutamine in the gastrointestinal tract: confirmation in a human study. Br J Surg. 1991 Apr;78(4):480-2. [Article]
- Morlion BJ, Stehle P, Wachtler P, Siedhoff HP, Koller M, Konig W, Furst P, Puchstein C: Total parenteral nutrition with glutamine dipeptide after major abdominal surgery: a randomized, double-blind, controlled study. Ann Surg. 1998 Feb;227(2):302-8. [Article]
- Jian ZM, Cao JD, Zhu XG, Zhao WX, Yu JC, Ma EL, Wang XR, Zhu MW, Shu H, Liu YW: The impact of alanyl-glutamine on clinical safety, nitrogen balance, intestinal permeability, and clinical outcome in postoperative patients: a randomized, double-blind, controlled study of 120 patients. JPEN J Parenter Enteral Nutr. 1999 Sep-Oct;23(5 Suppl):S62-6. [Article]
- Endari Approval Article [Link]
- FDA Approved Drug Products: Endari L-Glutamine Oral Powder [Link]
- External Links
- Human Metabolome Database
- HMDB0000641
- KEGG Drug
- D00015
- KEGG Compound
- C00064
- PubChem Compound
- 5961
- PubChem Substance
- 46505866
- ChemSpider
- 5746
- BindingDB
- 18121
- 4885
- ChEBI
- 18050
- ChEMBL
- CHEMBL930
- ZINC
- ZINC000001532526
- PharmGKB
- PA10090
- Guide to Pharmacology
- GtP Drug Page
- PDBe Ligand
- GLN
- PDRhealth
- PDRhealth Drug Page
- Wikipedia
- Glutamine
- FDA label
- Download (121 KB)
- MSDS
- Download (72.1 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample dataNot Available Active Not Recruiting Treatment Chronic Atrophic Gastritis (CAG) 1 somestatus stop reason just information to hide Not Available Completed Not Available Cachexia / Glutamine; Metabolic Disorder 1 somestatus stop reason just information to hide Not Available Completed Not Available Citrulline / Gastrointestinal Failure / Intra Abdominal Pressure / Multi-organ Failure 1 somestatus stop reason just information to hide Not Available Completed Prevention Posterior Lumbar Spinal Fusion Surgery 1 somestatus stop reason just information to hide Not Available Completed Treatment Autoimmune Disorder / Diabetes Mellitus / Endocrine System Diseases / Immune System Diseases / Metabolic Diseases / Metabolism Disorder, Glucose / Type 1 Diabetes Mellitus 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Nutritional restart pharmaceutical lp
- Packagers
- Emmaus Medical Inc.
- Key Co.
- Mason Distributors
- Medtrition Inc.
- Nestle Nutrition
- Spectrum Pharmaceuticals
- Dosage Forms
Form Route Strength Powder Oral Solution Parenteral Solution Intravenous 0.2 g Powder, for solution Oral 5 g/1 Tablet Oral Tablet Oral 1000 mg Syrup Oral Powder Oral 100 gr - Prices
Unit description Cost Unit L-glutamine crystals 3.76USD g Argiment packets 2.43USD packet L-glutamine 500 mg tablet 0.12USD tablet Glutamic-500 tablet 0.05USD tablet Impact glutamine liquid 0.05USD ml DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
Patent Number Pediatric Extension Approved Expires (estimated) Region US5288703 No 1994-02-22 2011-10-07 US
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 185.5 dec °C PhysProp water solubility 4.13E+004 mg/L (at 25 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992) logP -3.64 CHMELIK,J ET AL. (1991) logS -0.55 ADME Research, USCD pKa 2.17 MERCK INDEX (1996) - Predicted Properties
Property Value Source Water Solubility 97.8 mg/mL ALOGPS logP -3.3 ALOGPS logP -4 Chemaxon logS -0.17 ALOGPS pKa (Strongest Acidic) 2.15 Chemaxon pKa (Strongest Basic) 9.31 Chemaxon Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 4 Chemaxon Hydrogen Donor Count 3 Chemaxon Polar Surface Area 106.41 Å2 Chemaxon Rotatable Bond Count 4 Chemaxon Refractivity 33.11 m3·mol-1 Chemaxon Polarizability 13.87 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption - 0.5588 Blood Brain Barrier + 0.9604 Caco-2 permeable - 0.8957 P-glycoprotein substrate Non-substrate 0.7302 P-glycoprotein inhibitor I Non-inhibitor 0.964 P-glycoprotein inhibitor II Non-inhibitor 0.9919 Renal organic cation transporter Non-inhibitor 0.961 CYP450 2C9 substrate Non-substrate 0.845 CYP450 2D6 substrate Non-substrate 0.8496 CYP450 3A4 substrate Non-substrate 0.7544 CYP450 1A2 substrate Non-inhibitor 0.9583 CYP450 2C9 inhibitor Non-inhibitor 0.9741 CYP450 2D6 inhibitor Non-inhibitor 0.96 CYP450 2C19 inhibitor Non-inhibitor 0.9761 CYP450 3A4 inhibitor Non-inhibitor 0.8936 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9932 Ames test Non AMES toxic 0.7849 Carcinogenicity Non-carcinogens 0.9136 Biodegradation Ready biodegradable 0.8854 Rat acute toxicity 1.2587 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9953 hERG inhibition (predictor II) Non-inhibitor 0.9828
Spectra
- Mass Spec (NIST)
- Download (7.65 KB)
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 132.3790184 predictedDarkChem Lite v0.1.0 [M-H]- 132.2180184 predictedDarkChem Lite v0.1.0 [M-H]- 132.4088184 predictedDarkChem Lite v0.1.0 [M-H]- 132.2157184 predictedDarkChem Lite v0.1.0 [M-H]- 125.12114 predictedDeepCCS 1.0 (2019) [M+H]+ 133.3216184 predictedDarkChem Lite v0.1.0 [M+H]+ 132.9177184 predictedDarkChem Lite v0.1.0 [M+H]+ 133.3173184 predictedDarkChem Lite v0.1.0 [M+H]+ 132.4576184 predictedDarkChem Lite v0.1.0 [M+H]+ 128.94943 predictedDeepCCS 1.0 (2019) [M+Na]+ 132.5678184 predictedDarkChem Lite v0.1.0 [M+Na]+ 132.6081184 predictedDarkChem Lite v0.1.0 [M+Na]+ 132.4743184 predictedDarkChem Lite v0.1.0 [M+Na]+ 132.5830184 predictedDarkChem Lite v0.1.0 [M+Na]+ 138.0399 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- AntagonistSubstrate
- General Function
- This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity
- Specific Function
- ATP binding
- Gene Name
- CTPS1
- Uniprot ID
- P17812
- Uniprot Name
- CTP synthase 1
- Molecular Weight
- 66689.9 Da
References
- MacLeod TJ, Lunn FA, Bearne SL: The role of lysine residues 297 and 306 in nucleoside triphosphate regulation of E. coli CTP synthase: inactivation by 2',3'-dialdehyde ATP and mutational analyses. Biochim Biophys Acta. 2006 Feb;1764(2):199-210. Epub 2005 Dec 27. [Article]
- Taylor SD, Mirzaei F, Sharifi A, Bearne SL: Synthesis of methylene- and difluoromethylenephosphonate analogues of uridine-4-phosphate and 3-deazauridine-4-phosphate. J Org Chem. 2006 Dec 8;71(25):9420-30. [Article]
- Fijolek A, Hofer A, Thelander L: Expression, purification, characterization, and in vivo targeting of trypanosome CTP synthetase for treatment of African sleeping sickness. J Biol Chem. 2007 Apr 20;282(16):11858-65. Epub 2007 Feb 28. [Article]
- Martin E, Palmic N, Sanquer S, Lenoir C, Hauck F, Mongellaz C, Fabrega S, Nitschke P, Esposti MD, Schwartzentruber J, Taylor N, Majewski J, Jabado N, Wynn RF, Picard C, Fischer A, Arkwright PD, Latour S: CTP synthase 1 deficiency in humans reveals its central role in lymphocyte proliferation. Nature. 2014 Jun 12;510(7504):288-92. doi: 10.1038/nature13386. Epub 2014 May 28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine
- Specific Function
- 4 iron, 4 sulfur cluster binding
- Gene Name
- PPAT
- Uniprot ID
- Q06203
- Uniprot Name
- Amidophosphoribosyltransferase
- Molecular Weight
- 57398.52 Da
References
- Raushel FM, Thoden JB, Holden HM: The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia. Biochemistry. 1999 Jun 22;38(25):7891-9. doi: 10.1021/bi990871p. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Product of
- General Function
- Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (PubMed:36289327)
- Specific Function
- ATP binding
- Gene Name
- GLUL
- Uniprot ID
- P15104
- Uniprot Name
- Glutamine synthetase
- Molecular Weight
- 42064.15 Da
References
- Mong JA, Blutstein T: Estradiol modulation of astrocytic form and function: implications for hormonal control of synaptic communication. Neuroscience. 2006;138(3):967-75. Epub 2005 Dec 2. [Article]
- Rose C, Felipo V: Limited capacity for ammonia removal by brain in chronic liver failure: potential role of nitric oxide. Metab Brain Dis. 2005 Dec;20(4):275-83. [Article]
- Miguel-Hidalgo JJ: Withdrawal from free-choice ethanol consumption results in increased packing density of glutamine synthetase-immunoreactive astrocytes in the prelimbic cortex of alcohol-preferring rats. Alcohol Alcohol. 2006 Jul-Aug;41(4):379-85. Epub 2006 Feb 16. [Article]
- Chatauret N, Desjardins P, Zwingmann C, Rose C, Rao KV, Butterworth RF: Direct molecular and spectroscopic evidence for increased ammonia removal capacity of skeletal muscle in acute liver failure. J Hepatol. 2006 Jun;44(6):1083-8. Epub 2006 Jan 4. [Article]
- Tan S, Evans R, Singh B: Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops. Amino Acids. 2006 Mar;30(2):195-204. Epub 2006 Mar 20. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin
- Specific Function
- metal ion binding
- Gene Name
- F13A1
- Uniprot ID
- P00488
- Uniprot Name
- Coagulation factor XIII A chain
- Molecular Weight
- 83267.785 Da
References
- Mitkevich OV, Shainoff JR, DiBello PM, Yee VC, Teller DC, Smejkal GB, Bishop PD, Kolotushkina IS, Fickenscher K, Samokhin GP: Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIA by a cross-reacting antifibrinogen antibody. J Biol Chem. 1998 Jun 5;273(23):14387-91. [Article]
- Wolff C, Lai CS: Fluorescence energy transfer detects changes in fibronectin structure upon surface binding. Arch Biochem Biophys. 1989 Feb 1;268(2):536-45. [Article]
- Wolff C, Lai CS: Evidence that the two amino termini of plasma fibronectin are in close proximity: a fluorescence energy transfer study. Biochemistry. 1988 May 3;27(9):3483-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain (PubMed:30239721, PubMed:30575854, PubMed:30970188)
- Specific Function
- glutaminase activity
- Gene Name
- GLS
- Uniprot ID
- O94925
- Uniprot Name
- Glutaminase kidney isoform, mitochondrial
- Molecular Weight
- 73460.56 Da
References
- Masson J, Darmon M, Conjard A, Chuhma N, Ropert N, Thoby-Brisson M, Foutz AS, Parrot S, Miller GM, Jorisch R, Polan J, Hamon M, Hen R, Rayport S: Mice lacking brain/kidney phosphate-activated glutaminase have impaired glutamatergic synaptic transmission, altered breathing, disorganized goal-directed behavior and die shortly after birth. J Neurosci. 2006 Apr 26;26(17):4660-71. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation
- Specific Function
- glutaminase activity
- Gene Name
- GLS2
- Uniprot ID
- Q9UI32
- Uniprot Name
- Glutaminase liver isoform, mitochondrial
- Molecular Weight
- 66322.225 Da
References
- Sido B, Seel C, Hochlehnert A, Breitkreutz R, Droge W: Low intestinal glutamine level and low glutaminase activity in Crohn's disease: a rational for glutamine supplementation? Dig Dis Sci. 2006 Dec;51(12):2170-9. Epub 2006 Nov 1. [Article]
- Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I: Structure of a bacterial pyridoxal 5'-phosphate synthase complex. Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. [Article]
- Myers RS, Amaro RE, Luthey-Schulten ZA, Davisson VJ: Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry. 2005 Sep 13;44(36):11974-85. [Article]
- Benlloch M, Mena S, Ferrer P, Obrador E, Asensi M, Pellicer JA, Carretero J, Ortega A, Estrela JM: Bcl-2 and Mn-SOD antisense oligodeoxynucleotides and a glutamine-enriched diet facilitate elimination of highly resistant B16 melanoma cells by tumor necrosis factor-alpha and chemotherapy. J Biol Chem. 2006 Jan 6;281(1):69-79. Epub 2005 Nov 1. [Article]
- Campos-Sandoval JA, Lopez de la Oliva AR, Lobo C, Segura JA, Mates JM, Alonso FJ, Marquez J: Expression of functional human glutaminase in baculovirus system: affinity purification, kinetic and molecular characterization. Int J Biochem Cell Biol. 2007;39(4):765-73. Epub 2006 Dec 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:23941696, PubMed:31991788, PubMed:9252372). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:27270573, PubMed:7935379, PubMed:9252372, PubMed:28198360). Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:23941696, PubMed:24349085, PubMed:29618516, PubMed:30458214). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses (PubMed:18092889, PubMed:7592956, PubMed:7649299). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (PubMed:12506096). Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (PubMed:7935379, PubMed:9252372). In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (PubMed:23797785, PubMed:30867594). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (PubMed:30867594, PubMed:32273471). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (PubMed:30867594). Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (PubMed:32273471). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (PubMed:20547769, PubMed:9623982). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (PubMed:9623982). May also act as an isopeptidase cleaving the previously formed cross-links (PubMed:26250429, PubMed:27131890). Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:8943303)
- Specific Function
- calcium ion binding
- Gene Name
- TGM2
- Uniprot ID
- P21980
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase 2
- Molecular Weight
- 77328.21 Da
References
- Park SS, Kim JM, Kim DS, Kim IH, Kim SY: Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster. J Biol Chem. 2006 Nov 17;281(46):34965-72. Epub 2006 Sep 20. [Article]
- Keresztessy Z, Csosz E, Harsfalvi J, Csomos K, Gray J, Lightowlers RN, Lakey JH, Balajthy Z, Fesus L: Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2. Protein Sci. 2006 Nov;15(11):2466-80. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes
- Specific Function
- metal ion binding
- Gene Name
- TGM5
- Uniprot ID
- O43548
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase 5
- Molecular Weight
- 80777.115 Da
References
- Candi E, Paradisi A, Terrinoni A, Pietroni V, Oddi S, Cadot B, Jogini V, Meiyappan M, Clardy J, Finazzi-Agro A, Melino G: Transglutaminase 5 is regulated by guanine-adenine nucleotides. Biochem J. 2004 Jul 1;381(Pt 1):313-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
- Specific Function
- metal ion binding
- Gene Name
- TGM6
- Uniprot ID
- O95932
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase 6
- Molecular Weight
- 79311.745 Da
References
- Tatsukawa H, Takeuchi T, Shinoda Y, Hitomi K: Identification and characterization of substrates crosslinked by transglutaminases in liver and kidney fibrosis. Anal Biochem. 2020 Feb 13:113629. doi: 10.1016/j.ab.2020.113629. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. Involved in cell proliferation (PubMed:26220141)
- Specific Function
- identical protein binding
- Gene Name
- TGM1
- Uniprot ID
- P22735
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase K
- Molecular Weight
- 89786.14 Da
References
- Boeshans KM, Mueser TC, Ahvazi B: A three-dimensional model of the human transglutaminase 1: insights into the understanding of lamellar ichthyosis. J Mol Model. 2007 Jan;13(1):233-46. Epub 2006 Sep 23. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Associated with the mammalian reproductive process. Catalyzes the cross-linking of proteins and the conjugation of polyamines to specific proteins in the seminal tract
- Specific Function
- metal ion binding
- Gene Name
- TGM4
- Uniprot ID
- P49221
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase 4
- Molecular Weight
- 77144.595 Da
References
- Stenberg P, Curtis CG, Wing D, Tong YS, Credo RB, Gray A, Lorand L: Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines. Biochem J. 1975 Apr;147(1):155-63. [Article]
- Mosher DF: Labeling of a major fibroblast surface protein (fibronectin) catalyzed by blood coagulation factor XIIa. Biochim Biophys Acta. 1977 Mar 28;491(1):205-10. [Article]
- Coyne CP, Smith JE, Keeton K: Additive and synergistic pharmacologic inhibition of equine fibrinoligase (factor XIIIa*-like) biochemical activity. Am J Vet Res. 1992 Nov;53(11):2058-66. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath
- Specific Function
- acyltransferase activity
- Gene Name
- TGM3
- Uniprot ID
- Q08188
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase E
- Molecular Weight
- 76631.26 Da
References
- Chen BS, Wang MR, Xu X, Cai Y, Xu ZX, Han YL, Wu M: Transglutaminase-3, an esophageal cancer-related gene. Int J Cancer. 2000 Dec 15;88(6):862-5. [Article]
- Ikura K, Yu C, Nagao M, Sasaki R, Furuyoshi S, Kawabata N: Site-directed mutation in conserved anionic regions of guinea pig liver transglutaminase. Arch Biochem Biophys. 1995 Apr 20;318(2):307-13. [Article]
- Ahvazi B, Steinert PM: A model for the reaction mechanism of the transglutaminase 3 enzyme. Exp Mol Med. 2003 Aug 31;35(4):228-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
- Specific Function
- metal ion binding
- Gene Name
- TGM7
- Uniprot ID
- Q96PF1
- Uniprot Name
- Protein-glutamine gamma-glutamyltransferase Z
- Molecular Weight
- 79940.615 Da
References
- Tatsukawa H, Takeuchi T, Shinoda Y, Hitomi K: Identification and characterization of substrates crosslinked by transglutaminases in liver and kidney fibrosis. Anal Biochem. 2020 Feb 13:113629. doi: 10.1016/j.ab.2020.113629. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate
- Specific Function
- ATP binding
- Gene Name
- GMPS
- Uniprot ID
- P49915
- Uniprot Name
- GMP synthase [glutamine-hydrolyzing]
- Molecular Weight
- 76714.79 Da
References
- Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I: Structure of a bacterial pyridoxal 5'-phosphate synthase complex. Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. [Article]
- Myers RS, Amaro RE, Luthey-Schulten ZA, Davisson VJ: Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry. 2005 Sep 13;44(36):11974-85. [Article]
- Neuwirth M, Flicker K, Strohmeier M, Tews I, Macheroux P: Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry. 2007 May 1;46(17):5131-9. Epub 2007 Apr 5. [Article]
- Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I: Ammonia channel couples glutaminase with transamidase reactions in GatCAB. Science. 2006 Jun 30;312(5782):1954-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Not Available
- Specific Function
- asparagine synthase (glutamine-hydrolyzing) activity
- Gene Name
- ASNS
- Uniprot ID
- P08243
- Uniprot Name
- Asparagine synthetase [glutamine-hydrolyzing]
- Molecular Weight
- 64369.39 Da
References
- Li KK, Beeson WT 4th, Ghiviriga I, Richards NG: A convenient gHMQC-based NMR assay for investigating ammonia channeling in glutamine-dependent amidotransferases: studies of Escherichia coli asparagine synthetase B. Biochemistry. 2007 Apr 24;46(16):4840-9. Epub 2007 Mar 31. [Article]
- Al Sarraj J, Vinson C, Thiel G: Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP. Biol Chem. 2005 Sep;386(9):873-9. [Article]
- Sheppard K, Akochy PM, Salazar JC, Soll D: The Helicobacter pylori amidotransferase GatCAB is equally efficient in glutamine-dependent transamidation of Asp-tRNAAsn and Glu-tRNAGln. J Biol Chem. 2007 Apr 20;282(16):11866-73. Epub 2007 Feb 28. [Article]
- Barsch A, Carvalho HG, Cullimore JV, Niehaus K: GC-MS based metabolite profiling implies three interdependent ways of ammonium assimilation in Medicago truncatula root nodules. J Biotechnol. 2006 Dec 15;127(1):79-83. Epub 2006 Jun 21. [Article]
- Reinert RB, Oberle LM, Wek SA, Bunpo P, Wang XP, Mileva I, Goodwin LO, Aldrich CJ, Durden DL, McNurlan MA, Wek RC, Anthony TG: Role of glutamine depletion in directing tissue-specific nutrient stress responses to L-asparaginase. J Biol Chem. 2006 Oct 20;281(42):31222-33. Epub 2006 Aug 24. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others (PubMed:19338303, PubMed:28097769). Also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites (PubMed:7883047). Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (PubMed:7883047)
- Specific Function
- cysteine-S-conjugate beta-lyase activity
- Gene Name
- KYAT1
- Uniprot ID
- Q16773
- Uniprot Name
- Kynurenine--oxoglutarate transaminase 1
- Molecular Weight
- 47874.765 Da
References
- Fukushima T, Mitsuhashi S, Tomiya M, Iyo M, Hashimoto K, Toyo'oka T: Determination of kynurenic acid in human serum and its correlation with the concentration of certain amino acids. Clin Chim Acta. 2007 Feb;377(1-2):174-8. Epub 2006 Sep 30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate
- Specific Function
- ATP binding
- Gene Name
- PFAS
- Uniprot ID
- O15067
- Uniprot Name
- Phosphoribosylformylglycinamidine synthase
- Molecular Weight
- 144733.165 Da
References
- Jayaram HN, Lui MS, Plowman J, Pillwein K, Reardon MA, Elliott WL, Weber G: Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride. Cancer Chemother Pharmacol. 1990;26(2):88-92. [Article]
- Prajda N, Natsumeda Y, Ikegami T, Reardon MA, Szondy S, Hashimoto Y, Emrani J, Weber G: Enzymic programs of rat bone marrow and the impact of acivicin and tiazofurin. Biochem Pharmacol. 1988 Mar 1;37(5):875-80. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln)
- Specific Function
- ATP binding
- Gene Name
- GATB
- Uniprot ID
- O75879
- Uniprot Name
- Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
- Molecular Weight
- 61863.57 Da
References
- Nagao A, Suzuki T, Katoh T, Sakaguchi Y, Suzuki T: Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16209-14. doi: 10.1073/pnas.0907602106. Epub 2009 Sep 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins
- Specific Function
- carbohydrate derivative binding
- Gene Name
- GFPT2
- Uniprot ID
- O94808
- Uniprot Name
- Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2
- Molecular Weight
- 76929.885 Da
References
- Hu Y, Riesland L, Paterson AJ, Kudlow JE: Phosphorylation of mouse glutamine-fructose-6-phosphate amidotransferase 2 (GFAT2) by cAMP-dependent protein kinase increases the enzyme activity. J Biol Chem. 2004 Jul 16;279(29):29988-93. Epub 2004 May 7. [Article]
- Zitzler J, Link D, Schafer R, Liebetrau W, Kazinski M, Bonin-Debs A, Behl C, Buckel P, Brinkmann U: High-throughput functional genomics identifies genes that ameliorate toxicity due to oxidative stress in neuronal HT-22 cells: GFPT2 protects cells against peroxide. Mol Cell Proteomics. 2004 Aug;3(8):834-40. Epub 2004 Jun 4. [Article]
- DeHaven JE, Robinson KA, Nelson BA, Buse MG: A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes. 2001 Nov;50(11):2419-24. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate
- Specific Function
- aspartate binding
- Gene Name
- CAD
- Uniprot ID
- P27708
- Uniprot Name
- Multifunctional protein CAD
- Molecular Weight
- 242981.73 Da
References
- Moreno-Morcillo M, Grande-Garcia A, Ruiz-Ramos A, Del Cano-Ochoa F, Boskovic J, Ramon-Maiques S: Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis. Structure. 2017 Jun 6;25(6):912-923.e5. doi: 10.1016/j.str.2017.04.012. Epub 2017 May 25. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Glutamine--tRNA ligase (PubMed:26869582). Plays a critical role in brain development (PubMed:24656866)
- Specific Function
- ATP binding
- Gene Name
- QARS1
- Uniprot ID
- P47897
- Uniprot Name
- Glutamine--tRNA ligase
- Molecular Weight
- 87797.97 Da
References
- Balg C, Blais SP, Bernier S, Huot JL, Couture M, Lapointe J, Chenevert R: Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases. Bioorg Med Chem. 2007 Jan 1;15(1):295-304. Epub 2006 Sep 29. [Article]
- Fuchs BC, Bode BP: Stressing out over survival: glutamine as an apoptotic modulator. J Surg Res. 2006 Mar;131(1):26-40. Epub 2005 Sep 8. [Article]
- Yamasaki S, Nakamura S, Terada T, Shimizu K: Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop. Biophys J. 2007 Jan 1;92(1):192-200. Epub 2006 Oct 6. [Article]
- Uter NT, Perona JJ: Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit. Biochemistry. 2006 Jun 6;45(22):6858-65. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the final step of the nicotinamide adenine dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent amidation of deamido-NAD using L-glutamine as a nitrogen source
- Specific Function
- ATP binding
- Gene Name
- NADSYN1
- Uniprot ID
- Q6IA69
- Uniprot Name
- Glutamine-dependent NAD(+) synthetase
- Molecular Weight
- 79283.945 Da
References
- Wojcik M, Seidle HF, Bieganowski P, Brenner C: Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. J Biol Chem. 2006 Nov 3;281(44):33395-402. Epub 2006 Sep 5. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Symporter that cotransports short-chain neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane (PubMed:10891391, PubMed:20599747). The transport is elctrogenic, pH dependent and driven by the Na(+) electrochemical gradient (PubMed:10891391). Participates in the astroglia-derived glutamine transport into GABAergic interneurons for neurotransmitter GABA de novo synthesis (By similarity). May also contributes to amino acid transport in placental trophoblasts (PubMed:20599747). Also regulates synaptic plasticity (PubMed:12388062)
- Specific Function
- alanine
- Gene Name
- SLC38A1
- Uniprot ID
- Q9H2H9
- Uniprot Name
- Sodium-coupled neutral amino acid symporter 1
- Molecular Weight
- 54047.02 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10930503, PubMed:15774260, PubMed:15922329, PubMed:16621798). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (PubMed:10930503, PubMed:15774260). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity)
- Specific Function
- acidic amino acid transmembrane transporter activity
- Gene Name
- SLC38A2
- Uniprot ID
- Q96QD8
- Uniprot Name
- Sodium-coupled neutral amino acid symporter 2
- Molecular Weight
- 56025.375 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Symporter that cotransports specific neutral amino acids and sodium ions, coupled to an H(+) antiporter activity (PubMed:10823827). Mainly participates in the glutamate-GABA-glutamine cycle in brain where it transports L-glutamine from astrocytes in the intercellular space for the replenishment of both neurotransmitters glutamate and gamma-aminobutyric acid (GABA) in neurons and also functions as the major influx transporter in ganglion cells mediating the uptake of glutamine (By similarity). The transport activity is specific for L-glutamine, L-histidine and L-asparagine (PubMed:10823827). The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (By similarity). The transport is pH dependent, saturable, Li(+) tolerant and functions in both direction depending on the concentration gradients of its substrates and cotransported ions (PubMed:10823827). Also mediates an amino acid-gated H(+) conductance that is not stoichiometrically coupled to the amino acid transport but which influences the ionic gradients that drive the amino acid transport (By similarity). In addition, may play a role in nitrogen metabolism, amino acid homeostasis, glucose metabolism and renal ammoniagenesis (By similarity)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC38A3
- Uniprot ID
- Q99624
- Uniprot Name
- Sodium-coupled neutral amino acid transporter 3
- Molecular Weight
- 55772.405 Da
References
- Umapathy NS, Li W, Mysona BA, Smith SB, Ganapathy V: Expression and function of glutamine transporters SN1 (SNAT3) and SN2 (SNAT5) in retinal Muller cells. Invest Ophthalmol Vis Sci. 2005 Nov;46(11):3980-7. [Article]
- Conti F, Melone M: The glutamine commute: lost in the tube? Neurochem Int. 2006 May-Jun;48(6-7):459-64. Epub 2006 Mar 3. [Article]
- Gajewski M, Seaver B, Esslinger CS: Design, synthesis, and biological activity of novel triazole amino acids used to probe binding interactions between ligand and neutral amino acid transport protein SN1. Bioorg Med Chem Lett. 2007 Aug 1;17(15):4163-6. Epub 2007 May 23. [Article]
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (PubMed:17094966, PubMed:23756778, PubMed:26492990, PubMed:29872227, PubMed:34741534, PubMed:8702519). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (PubMed:23756778, PubMed:24953180). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (PubMed:32733894). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (PubMed:17094966). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC1A5
- Uniprot ID
- Q15758
- Uniprot Name
- Neutral amino acid transporter B(0)
- Molecular Weight
- 56597.64 Da
References
- Bungard CI, McGivan JD: Identification of the promoter elements involved in the stimulation of ASCT2 expression by glutamine availability in HepG2 cells and the probable involvement of FXR/RXR dimers. Arch Biochem Biophys. 2005 Nov 15;443(1-2):53-9. Epub 2005 Sep 15. [Article]
- Gegelashvili M, Rodriguez-Kern A, Pirozhkova I, Zhang J, Sung L, Gegelashvili G: High-affinity glutamate transporter GLAST/EAAT1 regulates cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes. Neurochem Int. 2006 May-Jun;48(6-7):611-5. Epub 2006 Mar 3. [Article]
- Oppedisano F, Pochini L, Galluccio M, Indiveri C: The glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: transport mechanism, regulation by ATP and characterization of the glutamine/glutamate antiport. Biochim Biophys Acta. 2007 Feb;1768(2):291-8. Epub 2006 Sep 16. [Article]
- Dun Y, Mysona B, Itagaki S, Martin-Studdard A, Ganapathy V, Smith SB: Functional and molecular analysis of D-serine transport in retinal Muller cells. Exp Eye Res. 2007 Jan;84(1):191-9. Epub 2006 Nov 13. [Article]
- McGivan JD, Bungard CI: The transport of glutamine into mammalian cells. Front Biosci. 2007 Jan 1;12:874-82. [Article]
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Amino acid transporter that plays an important role in the absorption of amino acids in the intestinal tract. Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner (PubMed:10446133). Transports non-alpha-amino acids such as beta-alanine with low affinity, and has a higher affinity for dipolar and cationic amino acids such as leucine and lysine (PubMed:18599538). Can also transport carnitine, butirylcarnitine and propionylcarnitine coupled to the transmembrane gradients of Na(+) and Cl(-) (PubMed:17855766)
- Specific Function
- (R)-carnitine transmembrane transporter activity
- Gene Name
- SLC6A14
- Uniprot ID
- Q9UN76
- Uniprot Name
- Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)
- Molecular Weight
- 72152.145 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids from inside the cells in exchange with neutral amino acids plus sodium ions and may participate in nitric oxide synthesis via the transport of L-arginine (PubMed:10080182, PubMed:10655553, PubMed:14603368, PubMed:15756301, PubMed:15776427, PubMed:17329401, PubMed:9829974, PubMed:9878049). Also mediates arginine transport in non-polarized cells, such as monocytes, and is essential for the correct function of these cells (PubMed:15280038, PubMed:31705628). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (By similarity). In vitro, Na(+) and Li(+), but also H(+), are cotransported with the neutral amino acids (By similarity)
- Specific Function
- basic amino acid transmembrane transporter activity
- Gene Name
- SLC7A7
- Uniprot ID
- Q9UM01
- Uniprot Name
- Y+L amino acid transporter 1
- Molecular Weight
- 55990.01 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (PubMed:10903140, PubMed:11311135, PubMed:14603368, PubMed:15756301, PubMed:16785209, PubMed:17329401, PubMed:19562367, PubMed:31705628, PubMed:9829974). Also exchanges L-arginine with L-lysine in a sodium-independent manner (PubMed:10903140). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (PubMed:10903140). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (PubMed:17197568). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC7A6
- Uniprot ID
- Q92536
- Uniprot Name
- Y+L amino acid transporter 2
- Molecular Weight
- 56826.87 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- The heterodimer with SLC3A2 functions as a sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine (PubMed:10049700, PubMed:10574970, PubMed:11557028, PubMed:11564694, PubMed:12117417, PubMed:12225859, PubMed:15769744, PubMed:18262359, PubMed:25998567, PubMed:30867591, PubMed:9751058). The heterodimer with SLC3A2 mediates the uptake of L-DOPA (By similarity). Functions as an amino acid exchanger (PubMed:11557028, PubMed:12117417, PubMed:12225859, PubMed:30867591). May play a role in the transport of L-DOPA across the blood-brain barrier (By similarity). May act as the major transporter of tyrosine in fibroblasts (Probable). May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier (By similarity). Can mediate the transport of thyroid hormones diiodothyronine (T2), triiodothyronine (T3) and thyroxine (T4) across the cell membrane (PubMed:11564694). When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes (PubMed:12117417). Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the membrane (PubMed:15769744)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC7A5
- Uniprot ID
- Q01650
- Uniprot Name
- Large neutral amino acids transporter small subunit 1
- Molecular Weight
- 55009.62 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Associates with SLC3A2 to form a functional heterodimeric complex that translocates small and large neutral amino acids with broad specificity and a stoichiometry of 1:1. Functions as amino acid antiporter mediating the influx of extracellular essential amino acids mainly in exchange with the efflux of highly concentrated intracellular amino acids (PubMed:10391915, PubMed:11311135, PubMed:11847106, PubMed:12716892, PubMed:15081149, PubMed:15918515, PubMed:29355479, PubMed:33298890, PubMed:34848541). Has relatively symmetrical selectivities but strongly asymmetrical substrate affinities at both the intracellular and extracellular sides of the transporter (PubMed:11847106). This asymmetry allows SLC7A8 to regulate intracellular amino acid pools (mM concentrations) by exchange with external amino acids (uM concentration range), equilibrating the relative concentrations of different amino acids across the plasma membrane instead of mediating their net uptake (PubMed:10391915, PubMed:11847106). May play an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney (PubMed:12716892). Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity (PubMed:12117417). Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane (PubMed:15769744). Imports the thyroid hormone diiodothyronine (T2) and to a smaller extent triiodothyronine (T3) but not rT 3 or thyroxine (T4) (By similarity). Mediates the uptake of L-DOPA (By similarity). May participate in auditory function (By similarity)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC7A8
- Uniprot ID
- Q9UHI5
- Uniprot Name
- Large neutral amino acids transporter small subunit 2
- Molecular Weight
- 58381.12 Da
References
- Umapathy NS, Li W, Mysona BA, Smith SB, Ganapathy V: Expression and function of glutamine transporters SN1 (SNAT3) and SN2 (SNAT5) in retinal Muller cells. Invest Ophthalmol Vis Sci. 2005 Nov;46(11):3980-7. [Article]
- Kirchhoff P, Dave MH, Remy C, Kosiek O, Busque SM, Dufner M, Geibel JP, Verrey F, Wagner CA: An amino acid transporter involved in gastric acid secretion. Pflugers Arch. 2006 Mar;451(6):738-48. Epub 2005 Nov 25. [Article]
- Ramadan T, Camargo SM, Herzog B, Bordin M, Pos KM, Verrey F: Recycling of aromatic amino acids via TAT1 allows efflux of neutral amino acids via LAT2-4F2hc exchanger. Pflugers Arch. 2007 Jun;454(3):507-16. Epub 2007 Feb 2. [Article]
- Broer S, Broer A, Hansen JT, Bubb WA, Balcar VJ, Nasrallah FA, Garner B, Rae C: Alanine metabolism, transport, and cycling in the brain. J Neurochem. 2007 Sep;102(6):1758-70. Epub 2007 May 14. [Article]
- Chubb S, Kingsland AL, Broer A, Broer S: Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2 light-chain dysfunction. Mol Membr Biol. 2006 May-Jun;23(3):255-67. [Article]
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Associates with SLC3A1 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1 (PubMed:16825196, PubMed:32494597, PubMed:32817565, PubMed:8663357). Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids (PubMed:16825196, PubMed:32494597, PubMed:8663357). Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine (PubMed:8663357). Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules
- Specific Function
- antiporter activity
- Gene Name
- SLC7A9
- Uniprot ID
- P82251
- Uniprot Name
- b(0,+)-type amino acid transporter 1
- Molecular Weight
- 53480.81 Da
References
- Bode BP: Recent molecular advances in mammalian glutamine transport. J Nutr. 2001 Sep;131(9 Suppl):2475S-85S; discussion 2486S-7S. doi: 10.1093/jn/131.9.2475S. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Sodium- and proton-independent thyroid hormones and aromatic acids transporter (PubMed:11827462, PubMed:18337592, PubMed:28754537). Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels (PubMed:18337592). Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa) (PubMed:11827462, PubMed:28754537). Plays an important role in homeostasis of aromatic amino acids (By similarity)
- Specific Function
- amino acid transmembrane transporter activity
- Gene Name
- SLC16A10
- Uniprot ID
- Q8TF71
- Uniprot Name
- Monocarboxylate transporter 10
- Molecular Weight
- 55492.07 Da
References
- Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. [Article]
Drug created at June 13, 2005 13:24 / Updated at August 02, 2024 07:22