Identification

Name
Aspartic acid
Accession Number
DB00128
Description

One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.

Type
Small Molecule
Groups
Approved, Nutraceutical
Structure
Thumb
Weight
Average: 133.1027
Monoisotopic: 133.037507717
Chemical Formula
C4H7NO4
Synonyms
  • (S)-2-aminobutanedioic acid
  • (S)-2-aminosuccinic acid
  • 2-Aminosuccinic acid
  • ácido aspártico
  • Acidum asparticum
  • Asp
  • Aspartic acid
  • D
  • L-Asp
  • L-Asparaginsäure
  • L-Aspartate
  • L-Aspartic acid
External IDs
  • FEMA NO. 3656

Pharmacology

Indication

There is no support for the claim that aspartates are exercise performance enhancers, i.e. ergogenic aids.

Contraindications & Blackbox Warnings
Learn about our commercial Contraindications & Blackbox Warnings data.
Learn More
Pharmacodynamics

L-aspartate is considered a non-essential amino acid, meaning that, under normal physiological conditions, sufficient amounts of the amino acid are synthesized in the body to meet the body's requirements. L-aspartate is formed by the transamination of the Krebs cycle intermediate oxaloacetate. The amino acid serves as a precursor for synthesis of proteins, oligopeptides, purines, pyrimidines, nucleic acids and L-arginine. L-aspartate is a glycogenic amino acid, and it can also promote energy production via its metabolism in the Krebs cycle. These latter activities were the rationale for the claim that supplemental aspartate has an anti-fatigue effect on skeletal muscle, a claim that was never confirmed.

Mechanism of action

There are also claims that L-aspartate has ergogenic effects, that it enhances performance in both prolonged exercise and short intensive exercise. It is hypothesized that L-aspartate, especially the potassium magnesium aspartate salt, spares stores of muscle glycogen and/or promotes a faster rate of glycogen resynthesis during exercise. It has also been hypothesized that L-aspartate can enhance short intensive exercise by serving as a substrate for energy production in the Krebs cycle and for stimulating the purine nucleotide cycle.

TargetActionsOrganism
URibonuclease pancreaticNot AvailableHumans
ULysozyme CNot AvailableHumans
UCalcium-binding mitochondrial carrier protein Aralar2Not AvailableHumans
UAspartate aminotransferase, cytoplasmicNot AvailableHumans
UAspartoacylaseNot AvailableHumans
UAsparagine synthetase [glutamine-hydrolyzing]
substrate
Humans
UArgininosuccinate synthaseNot AvailableHumans
UAminoacylase-1Not AvailableHumans
UAspartate aminotransferase, mitochondrialNot AvailableHumans
UAspartate--tRNA ligase, cytoplasmicNot AvailableHumans
UCalcium-binding mitochondrial carrier protein Aralar1Not AvailableHumans
UAspartyl/asparaginyl beta-hydroxylaseNot AvailableHumans
UMultifunctional protein ADE2
substrate
Humans
UAdenylosuccinate synthetase isozyme 2Not AvailableHumans
UExcitatory amino acid transporter 3Not AvailableHumans
UArgininosuccinate synthetase, isoform CRA_aNot AvailableHumans
UAspartate--tRNA ligase, mitochondrialNot AvailableHumans
UIsoaspartyl peptidase/L-asparaginaseNot AvailableHumans
UAdenylosuccinate Synthetases
substrate
Humans
Absorption

Absorbed from the small intestine by an active transport process

Volume of distribution
Not Available
Protein binding
Not Available
Metabolism
Not Available
Route of elimination
Not Available
Half-life
Not Available
Clearance
Not Available
Adverse Effects
Learn about our commercial Adverse Effects data.
Learn More
Toxicity

Mild gastrointestinal side effects including diarrhea. LD50 (rat) > 5,000 mg/kg.

Affected organisms
  • Humans and other mammals
Pathways
PathwayCategory
Malate-Aspartate ShuttleMetabolic
Adenylosuccinate Lyase DeficiencyDisease
Xanthine Dehydrogenase Deficiency (Xanthinuria)Disease
Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)Disease
HomocarnosinosisDisease
Carnosinuria, CarnosinemiaDisease
Creatine Deficiency, Guanidinoacetate Methyltransferase DeficiencyDisease
Hyperornithinemia with Gyrate Atrophy (HOGA)Disease
Xanthinuria Type IDisease
Mitochondrial DNA Depletion SyndromeDisease
Myoadenylate Deaminase DeficiencyDisease
Carbamoyl Phosphate Synthetase DeficiencyDisease
Argininosuccinic AciduriaDisease
Tyrosine MetabolismMetabolic
Ammonia RecyclingMetabolic
Arginine and Proline MetabolismMetabolic
Purine MetabolismMetabolic
Glutamate MetabolismMetabolic
Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)Disease
Purine Nucleoside Phosphorylase DeficiencyDisease
Tyrosinemia Type IDisease
Hyperinsulinism-Hyperammonemia SyndromeDisease
Hyperprolinemia Type IIDisease
Hyperprolinemia Type IDisease
Lesch-Nyhan Syndrome (LNS)Disease
Gout or Kelley-Seegmiller SyndromeDisease
Mercaptopurine Action PathwayDrug action
Disulfiram Action PathwayDrug action
L-Arginine:Glycine Amidinotransferase DeficiencyDisease
Adenine Phosphoribosyltransferase Deficiency (APRT)Disease
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.
Not Available
Food Interactions
No interactions found.

Products

Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
20% ProsolAspartic acid (0.6 g) + Alanine (2.76 g) + Arginine (1.96 g) + D-Methionine (0.76 g) + Glutamic acid (1.02 g) + Glycine (2.06 g) + Histidine (1.18 g) + Isoleucine (1.08 g) + L-Lysine (1.35 g) + Leucine (1.08 g) + Methionine (0.76 g) + Phenylalanine (1 g) + Proline (1.34 g) + Serine (1.02 g) + Threonine (0.98 g) + Tryptophan (0.32 g) + Tyrosine (0.05 g) + Valine (1.44 g)LiquidIntravenousBaxter Laboratories1996-10-09Not applicableCanada flag
Aminosyn IIAspartic acid (700 mg/100mL) + Alanine (993 mg/100mL) + Arginine (1018 mg/100mL) + Glutamic acid (738 mg/100mL) + Glycine (500 mg/100mL) + Histidine (300 mg/100mL) + Isoleucine (660 mg/100mL) + L-Lysine acetate (1050 mg/100mL) + Leucine (1000 mg/100mL) + Methionine (172 mg/100mL) + N-acetyltyrosine (270 mg/100mL) + Phenylalanine (298 mg/100mL) + Proline (722 mg/100mL) + Serine (530 mg/100mL) + Threonine (400 mg/100mL) + Tryptophan (200 mg/100mL) + Valine (500 mg/100mL)Injection, solutionIntravenousHospira, Inc.1991-12-192013-09-01US flag
Aminosyn IIAspartic acid (1050 mg) + Alanine (1490 mg) + Arginine (1527 mg) + Glutamic acid (1107 mg) + Glycine (750 mg) + Histidine (450 mg) + Isoleucine (990 mg) + L-Lysine acetate (1575 mg) + Leucine (1500 mg) + Methionine (258 mg) + N-acetyltyrosine (405 mg) + Phenylalanine (447 mg) + Proline (1083 mg) + Serine (795 mg) + Threonine (600 mg) + Tryptophan (300 mg) + Valine (750 mg)SolutionIntravenousIcu Medical Canada Inc1995-12-31Not applicableCanada flag
Aminosyn IIAspartic acid (595 mg/100mL) + Alanine (844 mg/100mL) + Arginine (865 mg/100mL) + Glutamic acid (627 mg/100mL) + Glycine (425 mg/100mL) + Histidine (255 mg/100mL) + Isoleucine (561 mg/100mL) + L-Lysine acetate (893 mg/100mL) + Leucine (850 mg/100mL) + Methionine (146 mg/100mL) + N-acetyltyrosine (230 mg/100mL) + Phenylalanine (253 mg/100mL) + Proline (614 mg/100mL) + Serine (450 mg/100mL) + Threonine (340 mg/100mL) + Tryptophan (170 mg/100mL) + Valine (425 mg/100mL)Injection, solutionIntravenousHospira, Inc.2005-07-292017-06-01US flag
Aminosyn IIAspartic acid (700 mg/100mL) + Alanine (993 mg/100mL) + Arginine (1018 mg/100mL) + Glutamic acid (738 mg/100mL) + Glycine (500 mg/100mL) + Histidine (300 mg/100mL) + Isoleucine (660 mg/100mL) + L-Lysine acetate (1050 mg/100mL) + Leucine (1000 mg/100mL) + Methionine (172 mg/100mL) + N-acetyltyrosine (270 mg/100mL) + Phenylalanine (298 mg/100mL) + Proline (722 mg/100mL) + Serine (530 mg/100mL) + Threonine (400 mg/100mL) + Tryptophan (200 mg/100mL) + Valine (500 mg/100mL)Injection, solutionIntravenousHospira, Inc.1991-12-192020-12-01US flag
Aminosyn IIAspartic acid (1050 mg/100mL) + Alanine (1490 mg/100mL) + Arginine (1527 mg/100mL) + Glutamic acid (1107 mg/100mL) + Glycine (750 mg/100mL) + Histidine (450 mg/100mL) + Isoleucine (990 mg/100mL) + L-Lysine acetate (1575 mg/100mL) + Leucine (1500 mg/100mL) + Methionine (258 mg/100mL) + N-acetyltyrosine (405 mg/100mL) + Phenylalanine (447 mg/100mL) + Proline (1083 mg/100mL) + Serine (795 mg/100mL) + Threonine (600 mg/100mL) + Tryptophan (300 mg/100mL) + Valine (750 mg/100mL)Injection, solutionIntravenousIcu Medical Inc.2019-11-01Not applicableUS flag
Aminosyn IIAspartic acid (1050 mg/100mL) + Alanine (1490 mg/100mL) + Arginine (1527 mg/100mL) + Glutamic acid (1107 mg/100mL) + Glycine (750 mg/100mL) + Histidine (450 mg/100mL) + Isoleucine (990 mg/100mL) + L-Lysine acetate (1575 mg/100mL) + Leucine (1500 mg/100mL) + Methionine (258 mg/100mL) + N-acetyltyrosine (405 mg/100mL) + Phenylalanine (447 mg/100mL) + Proline (1083 mg/100mL) + Serine (795 mg/100mL) + Threonine (600 mg/100mL) + Tryptophan (300 mg/100mL) + Valine (750 mg/100mL)Injection, solutionIntravenousHospira, Inc.1991-12-192023-12-01US flag
Aminosyn IIAspartic acid (700 mg) + Alanine (993 mg) + Arginine (1018 mg) + Glutamic acid (738 mg) + Glycine (500 mg) + Histidine (300 mg) + Isoleucine (660 mg) + L-Lysine (1050 mg) + Leucine (1000 mg) + Methionine (172 mg) + N-acetyltyrosine (270 mg) + Phenylalanine (298 mg) + Proline (722 mg) + Serine (530 mg) + Threonine (400 mg) + Tryptophan (200 mg) + Valine (500 mg)SolutionIntravenousIcu Medical Canada Inc1987-12-31Not applicableCanada flag
Aminosyn IIAspartic acid (1050 mg/100mL) + Alanine (1490 mg/100mL) + Arginine (1527 mg/100mL) + Glutamic acid (1107 mg/100mL) + Glycine (750 mg/100mL) + Histidine (450 mg/100mL) + Isoleucine (990 mg/100mL) + L-Lysine acetate (1575 mg/100mL) + Leucine (1500 mg/100mL) + Methionine (258 mg/100mL) + N-acetyltyrosine (405 mg/100mL) + Phenylalanine (447 mg/100mL) + Proline (1083 mg/100mL) + Serine (795 mg/100mL) + Threonine (600 mg/100mL) + Tryptophan (300 mg/100mL) + Valine (750 mg/100mL)Injection, solutionIntravenousHospira, Inc.1991-12-192011-10-01US flag
Aminosyn IIAspartic acid (490 mg/100mL) + Alanine (695 mg/100mL) + Arginine (713 mg/100mL) + Glutamic acid (517 mg/100mL) + Glycine (350 mg/100mL) + Histidine (210 mg/100mL) + Isoleucine (462 mg/100mL) + L-Lysine acetate (735 mg/100mL) + Leucine (700 mg/100mL) + Methionine (120 mg/100mL) + N-acetyltyrosine (189 mg/100mL) + Phenylalanine (209 mg/100mL) + Proline (505 mg/100mL) + Serine (371 mg/100mL) + Threonine (280 mg/100mL) + Tryptophan (140 mg/100mL) + Valine (350 mg/100mL)Injection, solutionIntravenousHospira, Inc.2005-11-012010-12-01US flag
Unapproved/Other Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
PrimeneAspartic acid (1.5 g/250mL) + Alanine (2 g/250mL) + Arginine (2.1 g/250mL) + Cysteine (0.47 g/250mL) + Glutamic acid (2.5 g/250mL) + Glycine (1 g/250mL) + Histidine (0.95 g/250mL) + Isoleucine (1.675 g/250mL) + L-Lysine (2.75 g/250mL) + Leucine (2.5 g/250mL) + Methionine (0.6 g/250mL) + Ornithine hydrochloride (0.8 g/250mL) + Phenylalanine (1.05 g/250mL) + Proline (0.75 g/250mL) + Serine (1 g/250mL) + Taurine (0.15 g/250mL) + Threonine (0.9 g/250mL) + Tryptophan (0.5 g/250mL) + Tyrosine (0.11 g/250mL) + Valine (1.9 g/250mL)Injection, solutionIntravenousBaxter Healthcare Corporation2017-11-222019-05-31US flag

Categories

Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
This compound belongs to the class of organic compounds known as aspartic acid and derivatives. These are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
Kingdom
Organic compounds
Super Class
Organic acids and derivatives
Class
Carboxylic acids and derivatives
Sub Class
Amino acids, peptides, and analogues
Direct Parent
Aspartic acid and derivatives
Alternative Parents
L-alpha-amino acids / Fatty acids and conjugates / Dicarboxylic acids and derivatives / Amino acids / Carboxylic acids / Organopnictogen compounds / Organic oxides / Monoalkylamines / Hydrocarbon derivatives / Carbonyl compounds
Substituents
Aliphatic acyclic compound / Alpha-amino acid / Amine / Amino acid / Aspartic acid or derivatives / Carbonyl group / Carboxylic acid / Dicarboxylic acid or derivatives / Fatty acid / Hydrocarbon derivative
Molecular Framework
Aliphatic acyclic compounds
External Descriptors
aspartate family amino acid, proteinogenic amino acid, L-alpha-amino acid, aspartic acid (CHEBI:17053) / Common amino acids, Amino acids (C00049)

Chemical Identifiers

UNII
30KYC7MIAI
CAS number
56-84-8
InChI Key
CKLJMWTZIZZHCS-REOHCLBHSA-N
InChI
InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1
IUPAC Name
(2S)-2-aminobutanedioic acid
SMILES
N[[email protected]@H](CC(O)=O)C(O)=O

References

Synthesis Reference

Nguyen-Cong Duc, "Method of making L-aspartic acid from fumaric acid." U.S. Patent US3933586, issued August, 1965.

US3933586
General References
Not Available
Human Metabolome Database
HMDB0000191
KEGG Drug
D00013
KEGG Compound
C00049
PubChem Compound
5960
PubChem Substance
46507997
ChemSpider
5745
BindingDB
18125
RxNav
1169
ChEBI
17053
ChEMBL
CHEMBL274323
ZINC
ZINC000000895032
PharmGKB
PA448494
Guide to Pharmacology
GtP Drug Page
PDBe Ligand
IAS
PDRhealth
PDRhealth Drug Page
Wikipedia
Aspartic_acid
PDB Entries
1at6 / 1c9p / 1dlg / 1dy5 / 1ejc / 1ejd / 1eyn / 1h0i / 1jg3 / 1lsq
show 43 more
MSDS
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Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
4CompletedPreventionHepatic Encephalopathy (HE)1
4CompletedTreatmentCirrhosis of the Liver / Hepatic Encephalopathy (HE)1
4RecruitingTreatmentNasal and Nasal-type NK/T-cell Lymphoma1
4TerminatedSupportive CareParenteral Nutrition (No Primary Condition Studied)1
4WithdrawnSupportive CareMalnutrition1
3Active Not RecruitingTreatmentAcute Lymphoblastic Leukaemias (ALL) / Acute Undifferentiated Leukemia (AUL) / Childhood T Acute Lymphoblastic Leukemia / T-cell Childhood Acute Lymphoblastic Leukemia / Untreated Childhood Acute Lymphoblastic Leukemia1
3Active Not RecruitingTreatmentAcute Myeloid Leukemia (AML) / Granulocytic Sarcoma / Leukaemia cutis / Myeloid Neoplasm1
3Active Not RecruitingTreatmentB-cell Childhood Acute Lymphoblastic Leukemia / Intermediate Risk Recurrent Childhood Acute Lymphoblastic Leukemia / L1 Childhood Acute Lymphoblastic Leukemia / L2 Childhood Acute Lymphoblastic Leukemia1
3Active Not RecruitingTreatmentRecurrent B Acute Lymphoblastic Leukemia1
3Active Not RecruitingTreatmentT Acute Lymphoblastic Leukemia / T Lymphoblastic Lymphoma1

Pharmacoeconomics

Manufacturers
Not Available
Packagers
  • Spectrum Pharmaceuticals
Dosage Forms
FormRouteStrength
SolutionIntravenous2.453 g
Solution, concentrateIntravenous5 g
Injection, solutionIntravenous
Injection, emulsionIntravenous
InjectionIntravenous110 g
InjectionIntravenous165 g
InjectionIntravenous220 g
InjectionIntravenous275 g
InjectionIntravenous107 g
InjectionIntravenous143 g
InjectionIntravenous178 g
Injection, solution, concentrateIntravenous
EmulsionIntravenous1.83 g
InjectionIntravenous1.03 g
EmulsionIntravenous20 mg
EmulsionIntravenous16 g
EmulsionIntravenous4 g
SolutionIntravenous7.14 g
SolutionIntravenous9.52 g
SolutionIntravenous11.9 g
EmulsionIntravenous6.41 g
EmulsionIntravenous9.61 g
EmulsionIntravenous12.82 g
SolutionIntravenous8.24 g
SolutionIntravenous12.36 g
SolutionIntravenous16.48 g
EmulsionIntravenous
EmulsionIntravenous3 g
Injection, solutionIntravenous0.49 %
SolutionIntravenous
InjectionIntravenous0.67 g/100ml
LiquidIntravenous
SolutionIntravenous434 mg
SolutionIntravenous12 g/L
SolutionIntravenous16 g/L
SolutionIntravenous5.1 g/16g N
Prices
Unit descriptionCostUnit
L-aspartic acid powder2.46USD g
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Not Available

Properties

State
Solid
Experimental Properties
PropertyValueSource
melting point (°C)270 °CPhysProp
water solubility5390 mg/L (at 25 °C)YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP-3.89CHMELIK,J ET AL. (1991)
pKa2.01 (at 0 °C)KORTUM,G ET AL (1961)
Predicted Properties
PropertyValueSource
Water Solubility142.0 mg/mLALOGPS
logP-3.5ALOGPS
logP-3.5ChemAxon
logS0.03ALOGPS
pKa (Strongest Acidic)1.7ChemAxon
pKa (Strongest Basic)9.61ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count5ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area100.62 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity26.53 m3·mol-1ChemAxon
Polarizability11.28 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET Features
PropertyValueProbability
Human Intestinal Absorption-0.5825
Blood Brain Barrier-0.6594
Caco-2 permeable-0.8271
P-glycoprotein substrateNon-substrate0.7668
P-glycoprotein inhibitor INon-inhibitor0.9714
P-glycoprotein inhibitor IINon-inhibitor0.9916
Renal organic cation transporterNon-inhibitor0.9672
CYP450 2C9 substrateNon-substrate0.856
CYP450 2D6 substrateNon-substrate0.8541
CYP450 3A4 substrateNon-substrate0.7916
CYP450 1A2 substrateNon-inhibitor0.9605
CYP450 2C9 inhibitorNon-inhibitor0.9657
CYP450 2D6 inhibitorNon-inhibitor0.9547
CYP450 2C19 inhibitorNon-inhibitor0.973
CYP450 3A4 inhibitorNon-inhibitor0.9372
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity1.0
Ames testNon AMES toxic0.9133
CarcinogenicityNon-carcinogens0.8906
BiodegradationReady biodegradable0.9088
Rat acute toxicity1.1037 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9849
hERG inhibition (predictor II)Non-inhibitor0.9795
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Download (2.96 KB)
Spectra
SpectrumSpectrum TypeSplash Key
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)GC-MSsplash10-0f89-0960000000-5a6a6cb21e9fc0875f84
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)GC-MSsplash10-0f89-0950000000-51399a8446c394459765
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)GC-MSsplash10-0f89-0950000000-f07e7f52b3c31fd119f5
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)GC-MSsplash10-0f89-0950000000-9e175dfa17a8b17a72d2
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)GC-MSsplash10-0f89-0950000000-f4475587d5a3b20bfc58
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)GC-MSsplash10-00di-9430000000-0cac9a97e698db1672b5
GC-MS Spectrum - GC-MS (2 TMS)GC-MSsplash10-03yi-1900000000-ea61b8526ee02ae79b66
GC-MS Spectrum - GC-MS (3 TMS)GC-MSsplash10-0f89-1890000000-7da576c8129142b71a1b
GC-MS Spectrum - GC-MS (4 TMS)GC-MSsplash10-0pb9-0981000000-ad23d55e348f55115f00
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSNot Available
GC-MS Spectrum - EI-BGC-MSsplash10-001i-0590000000-13cc5a7841854e97f68b
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0f89-0960000000-5a6a6cb21e9fc0875f84
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0f89-0950000000-51399a8446c394459765
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0f89-0950000000-f07e7f52b3c31fd119f5
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0f89-0950000000-9e175dfa17a8b17a72d2
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0f89-0950000000-f4475587d5a3b20bfc58
GC-MS Spectrum - GC-EI-QQGC-MSsplash10-0g4i-6946100000-0ae49e3be0f2f1f92065
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00di-9430000000-0cac9a97e698db1672b5
GC-MS Spectrum - GC-MSGC-MSsplash10-03yi-1900000000-ea61b8526ee02ae79b66
GC-MS Spectrum - GC-MSGC-MSsplash10-0f89-1890000000-7da576c8129142b71a1b
GC-MS Spectrum - GC-MSGC-MSsplash10-0pb9-0981000000-ad23d55e348f55115f00
MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)LC-MS/MSsplash10-0079-9300000000-92f9914d94078d96f5cf
MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)LC-MS/MSsplash10-00di-9000000000-c467d10f2b7e21ed1734
MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)LC-MS/MSsplash10-00dl-9000000000-87f0c58226f5a2f3ac8a
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-00di-0900000000-fde7ef1951fddff4b817
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0uk9-8900000000-2d7e5609618437e59272
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000i-9000000000-4b43567f4a446aed0828
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-014i-4900000000-45382d9abd25be948e5b
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-001i-0900000000-3f39a9b758e282358ac0
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-014i-3900000000-44d361ad09ff9a30dd14
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000i-9000000000-18e1dba62e6b803e17b8
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0002-0930000000-d97f9518a2d516d830c5
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-02ai-0962100000-909bb894b2c1318afee4
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-00di-9000000000-f2059dd438fcf62f62e1
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-03dr-7900000000-8b7b89ed34530e331024
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-014i-0190000000-58a78949f4b93de22aab
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0921000000-214b6b969fdc4216ca71
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-03dr-6900000000-4918748927dd097d2879
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0900000000-88dc2f1093f261e76201
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-004i-0290000000-a8856f56645a2961baac
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, NegativeLC-MS/MSsplash10-001i-0900000000-8cf9870557ca9adc3374
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, NegativeLC-MS/MSsplash10-000i-9400000000-81b2804a712625a2d9c4
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, NegativeLC-MS/MSsplash10-000i-9000000000-9bf77ba12ad952f84ac0
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, NegativeLC-MS/MSsplash10-00di-9000000000-e08bfb96c5fd8c9b9db7
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, NegativeLC-MS/MSsplash10-0006-9000000000-876e30f6c9ed061091fe
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, PositiveLC-MS/MSsplash10-00dl-9000000000-6c0d44d4e3853e5701a3
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, PositiveLC-MS/MSsplash10-00di-9000000000-95ddfd41454f63de9b05
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, PositiveLC-MS/MSsplash10-00di-9000000000-836341c418f94179fa14
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, PositiveLC-MS/MSsplash10-00lr-3900000000-ee3d722db4f8e0e1b9d3
LC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, PositiveLC-MS/MSsplash10-0006-9000000000-93fc8f80fb44ca0b910d
MS/MS Spectrum - CE-ESI-TOF (CE-system connected to 6210 Time-of-Flight MS, Agilent) , PositiveLC-MS/MSsplash10-001i-0900000000-90c9c5c165a18a64dbb3
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSNot Available
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-001i-0900000000-8cf9870557ca9adc3374
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-000i-9400000000-8769e48d9bcd1478d135
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-000i-9000000000-9bf77ba12ad952f84ac0
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-00di-9000000000-ef4738829a28310574c5
LC-MS/MS Spectrum - LC-ESI-QQ , negativeLC-MS/MSsplash10-0006-9000000000-876e30f6c9ed061091fe
LC-MS/MS Spectrum - LC-ESI-ITFT , negativeLC-MS/MSsplash10-00di-9000000000-f2059dd438fcf62f62e1
LC-MS/MS Spectrum - LC-ESI-ITFT , negativeLC-MS/MSsplash10-03dr-7900000000-8b7b89ed34530e331024
LC-MS/MS Spectrum - LC-ESI-ITFT , negativeLC-MS/MSsplash10-03dr-6900000000-4918748927dd097d2879
LC-MS/MS Spectrum - LC-ESI-ITFT , negativeLC-MS/MSsplash10-001i-0900000000-88dc2f1093f261e76201
LC-MS/MS Spectrum - LC-ESI-QQ , positiveLC-MS/MSsplash10-00dl-9000000000-6c0d44d4e3853e5701a3
LC-MS/MS Spectrum - LC-ESI-QQ , positiveLC-MS/MSsplash10-00di-9000000000-fb577022eba9d463f932
LC-MS/MS Spectrum - LC-ESI-QQ , positiveLC-MS/MSsplash10-00di-9000000000-836341c418f94179fa14
LC-MS/MS Spectrum - LC-ESI-QQ , positiveLC-MS/MSsplash10-00lr-3900000000-3e388b41b4cd2130e962
LC-MS/MS Spectrum - LC-ESI-QQ , positiveLC-MS/MSsplash10-0006-9000000000-93fc8f80fb44ca0b910d
LC-MS/MS Spectrum - LC-ESI-ITFT , positiveLC-MS/MSsplash10-000i-9000000000-4b43567f4a446aed0828
LC-MS/MS Spectrum - LC-ESI-ITFT , positiveLC-MS/MSsplash10-014i-4900000000-45382d9abd25be948e5b
LC-MS/MS Spectrum - LC-ESI-ITFT , positiveLC-MS/MSsplash10-014i-3900000000-44d361ad09ff9a30dd14
1H NMR Spectrum1D NMRNot Applicable
13C NMR Spectrum1D NMRNot Applicable
1H NMR Spectrum1D NMRNot Applicable
[1H,1H] 2D NMR Spectrum2D NMRNot Applicable
[1H,13C] 2D NMR Spectrum2D NMRNot Applicable

Targets

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Ribonuclease a activity
Specific Function
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
Gene Name
RNASE1
Uniprot ID
P07998
Uniprot Name
Ribonuclease pancreatic
Molecular Weight
17644.125 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Lysozyme activity
Specific Function
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Gene Name
LYZ
Uniprot ID
P61626
Uniprot Name
Lysozyme C
Molecular Weight
16536.885 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Transporter activity
Specific Function
Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle.
Gene Name
SLC25A13
Uniprot ID
Q9UJS0
Uniprot Name
Calcium-binding mitochondrial carrier protein Aralar2
Molecular Weight
74174.95 Da
References
  1. Contreras L, Gomez-Puertas P, Iijima M, Kobayashi K, Saheki T, Satrustegui J: Ca2+ Activation kinetics of the two aspartate-glutamate mitochondrial carriers, aralar and citrin: role in the heart malate-aspartate NADH shuttle. J Biol Chem. 2007 Mar 9;282(10):7098-106. Epub 2007 Jan 9. [PubMed:17213189]
  2. Saheki T, Iijima M, Li MX, Kobayashi K, Horiuchi M, Ushikai M, Okumura F, Meng XJ, Inoue I, Tajima A, Moriyama M, Eto K, Kadowaki T, Sinasac DS, Tsui LC, Tsuji M, Okano A, Kobayashi T: Citrin/mitochondrial glycerol-3-phosphate dehydrogenase double knock-out mice recapitulate features of human citrin deficiency. J Biol Chem. 2007 Aug 24;282(34):25041-52. Epub 2007 Jun 25. [PubMed:17591776]
  3. Satrustegui J, Pardo B, Del Arco A: Mitochondrial transporters as novel targets for intracellular calcium signaling. Physiol Rev. 2007 Jan;87(1):29-67. [PubMed:17237342]
  4. Ikeda S: [Adult-onset citrullinemia]. Brain Nerve. 2007 Jan;59(1):59-66. [PubMed:17354380]
  5. Ikeda S: [Adult-onset citrullinemia]. No To Shinkei. 2007 Jan;59(1):59-66. [PubMed:17228780]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Pyridoxal phosphate binding
Specific Function
Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a sca...
Gene Name
GOT1
Uniprot ID
P17174
Uniprot Name
Aspartate aminotransferase, cytoplasmic
Molecular Weight
46247.14 Da
References
  1. Tordjman J, Leroyer S, Chauvet G, Quette J, Chauvet C, Tomkiewicz C, Chapron C, Barouki R, Forest C, Aggerbeck M, Antoine B: Cytosolic aspartate aminotransferase, a new partner in adipocyte glyceroneogenesis and an atypical target of thiazolidinedione. J Biol Chem. 2007 Aug 10;282(32):23591-602. Epub 2007 Jun 1. [PubMed:17545671]
  2. Girgin S, Gedik E, Tacyildiz IH, Akgun Y, Bac B, Uysal E: Factors affecting morbidity and mortality in gangrenous cholecystitis. Acta Chir Belg. 2006 Sep-Oct;106(5):545-9. [PubMed:17168267]
  3. Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R: Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain. J Neurochem. 2007 Jul;102(1):103-11. Epub 2007 Apr 17. [PubMed:17442055]
  4. Wu ZM, Wen T, Tan YF, Liu Y, Ren F, Wu H: Effects of salvianolic acid a on oxidative stress and liver injury induced by carbon tetrachloride in rats. Basic Clin Pharmacol Toxicol. 2007 Feb;100(2):115-20. [PubMed:17244260]
  5. Zappacosta B, Manni A, Persichilli S, Boari A, Scribano D, Minucci A, Raffaelli L, Giardina B, De Sole P: Salivary thiols and enzyme markers of cell damage in periodontal disease. Clin Biochem. 2007 Jun;40(9-10):661-5. Epub 2007 Jan 26. [PubMed:17328883]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Metal ion binding
Specific Function
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maint...
Gene Name
ASPA
Uniprot ID
P45381
Uniprot Name
Aspartoacylase
Molecular Weight
35734.79 Da
References
  1. Wang J, Matalon R, Bhatia G, Wu G, Li H, Liu T, Lu ZH, Ledeen RW: Bimodal occurrence of aspartoacylase in myelin and cytosol of brain. J Neurochem. 2007 Apr;101(2):448-57. Epub 2007 Jan 24. [PubMed:17254025]
  2. Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr: Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):456-61. Epub 2006 Dec 28. [PubMed:17194761]
  3. Janson CG, McPhee SW, Francis J, Shera D, Assadi M, Freese A, Hurh P, Haselgrove J, Wang DJ, Bilaniuk L, Leone P: Natural history of Canavan disease revealed by proton magnetic resonance spectroscopy (1H-MRS) and diffusion-weighted MRI. Neuropediatrics. 2006 Aug;37(4):209-21. [PubMed:17177147]
  4. Srikanth SG, Chandrashekar HS, Nagarajan K, Jayakumar PN: Restricted diffusion in Canavan disease. Childs Nerv Syst. 2007 Apr;23(4):465-8. Epub 2007 Jan 12. [PubMed:17219235]
  5. Moffett JR, Ross B, Arun P, Madhavarao CN, Namboodiri AM: N-Acetylaspartate in the CNS: from neurodiagnostics to neurobiology. Prog Neurobiol. 2007 Feb;81(2):89-131. Epub 2007 Jan 5. [PubMed:17275978]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Protein homodimerization activity
Specific Function
Not Available
Gene Name
ASNS
Uniprot ID
P08243
Uniprot Name
Asparagine synthetase [glutamine-hydrolyzing]
Molecular Weight
64369.39 Da
References
  1. Yu Q, Wang X, Wang L, Zheng J, Wang J, Wang B: Knockdown of asparagine synthetase (ASNS) suppresses cell proliferation and inhibits tumor growth in gastric cancer cells. Scand J Gastroenterol. 2016 Oct;51(10):1220-6. doi: 10.1080/00365521.2016.1190399. Epub 2016 Jun 2. [PubMed:27251594]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Toxic substance binding
Specific Function
Is indirectly involved in the control of blood pressure.
Gene Name
ASS1
Uniprot ID
P00966
Uniprot Name
Argininosuccinate synthase
Molecular Weight
46530.055 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Flam BR, Eichler DC, Solomonson LP: Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle. Nitric Oxide. 2007 Nov-Dec;17(3-4):115-21. Epub 2007 Aug 3. [PubMed:17869551]
  4. Ben-Yoseph Y, Mitchell DA: Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of citrulline to arginine in intact fibroblasts. Clin Chim Acta. 1989 Aug 15;183(2):125-33. [PubMed:2791302]
  5. Shen LJ, Beloussow K, Shen WC: Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline-arginine regeneration pathway. Biochem Pharmacol. 2005 Jan 1;69(1):97-104. [PubMed:15588718]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Metallopeptidase activity
Specific Function
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Gene Name
ACY1
Uniprot ID
Q03154
Uniprot Name
Aminoacylase-1
Molecular Weight
45884.705 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Mitta M, Ohnogi H, Yamamoto A, Kato I, Sakiyama F, Tsunasawa S: The primary structure of porcine aminoacylase 1 deduced from cDNA sequence. J Biochem. 1992 Dec;112(6):737-42. [PubMed:1284246]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange betwe...
Gene Name
GOT2
Uniprot ID
P00505
Uniprot Name
Aspartate aminotransferase, mitochondrial
Molecular Weight
47517.285 Da
References
  1. Collier RH, Kohlhaw G: Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli. J Bacteriol. 1972 Oct;112(1):365-71. [PubMed:4404056]
  2. Grell EH: Genetic analysis of aspartate aminotransferase isozymes from hybrids between Drosophila melanogaster and Drosophila simulans and mutagen-induced isozyme variants. Genetics. 1976 Aug;83(4):753-64. [PubMed:823072]
  3. Recasens M, Mandel P: Similarities between cysteinesulphinate transaminase and aspartate aminotransferase. Ciba Found Symp. 1979;(72):259-70. [PubMed:261660]
  4. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [PubMed:10592235]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Poly(a) rna binding
Specific Function
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of...
Gene Name
DARS
Uniprot ID
P14868
Uniprot Name
Aspartate--tRNA ligase, cytoplasmic
Molecular Weight
57135.8 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Eiler S, Dock-Bregeon A, Moulinier L, Thierry JC, Moras D: Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. EMBO J. 1999 Nov 15;18(22):6532-41. [PubMed:10562565]
  4. Fender A, Sauter C, Messmer M, Putz J, Giege R, Florentz C, Sissler M: Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system. J Biol Chem. 2006 Jun 9;281(23):15980-6. Epub 2006 Apr 5. [PubMed:16597625]
  5. Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry JC, Moras D: The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J. 1994 Jan 15;13(2):327-37. [PubMed:8313877]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
L-glutamate transmembrane transporter activity
Specific Function
Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle.
Gene Name
SLC25A12
Uniprot ID
O75746
Uniprot Name
Calcium-binding mitochondrial carrier protein Aralar1
Molecular Weight
74761.225 Da
References
  1. Correia C, Coutinho AM, Diogo L, Grazina M, Marques C, Miguel T, Ataide A, Almeida J, Borges L, Oliveira C, Oliveira G, Vicente AM: Brief report: High frequency of biochemical markers for mitochondrial dysfunction in autism: no association with the mitochondrial aspartate/glutamate carrier SLC25A12 gene. J Autism Dev Disord. 2006 Nov;36(8):1137-40. [PubMed:17151801]
  2. Contreras L, Gomez-Puertas P, Iijima M, Kobayashi K, Saheki T, Satrustegui J: Ca2+ Activation kinetics of the two aspartate-glutamate mitochondrial carriers, aralar and citrin: role in the heart malate-aspartate NADH shuttle. J Biol Chem. 2007 Mar 9;282(10):7098-106. Epub 2007 Jan 9. [PubMed:17213189]
  3. Satrustegui J, Contreras L, Ramos M, Marmol P, del Arco A, Saheki T, Pardo B: Role of aralar, the mitochondrial transporter of aspartate-glutamate, in brain N-acetylaspartate formation and Ca(2+) signaling in neuronal mitochondria. J Neurosci Res. 2007 Nov 15;85(15):3359-66. [PubMed:17497669]
  4. Satrustegui J, Pardo B, Del Arco A: Mitochondrial transporters as novel targets for intracellular calcium signaling. Physiol Rev. 2007 Jan;87(1):29-67. [PubMed:17237342]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Structural molecule activity
Specific Function
Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.Isoform 8: membrane-bound Ca(2+)-sensing protein, which is a...
Gene Name
ASPH
Uniprot ID
Q12797
Uniprot Name
Aspartyl/asparaginyl beta-hydroxylase
Molecular Weight
85862.095 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Whiteman P, Marks C, Freese E: The sodium effect of Bacillus subtilis growth on aspartate. J Gen Microbiol. 1980 Aug;119(2):493-504. [PubMed:6785382]
  4. Iijima T, Diesterhaft MD, Freese E: Sodium effect of growth on aspartate and genetic analysis of a Bacillus subtilis mutant with high aspartase activity. J Bacteriol. 1977 Mar;129(3):1440-7. [PubMed:403177]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
Curator comments
Literature suggests that aspartic acid targets the phosphoribosylaminoimidazole-succinocarboxamide synthase domain of the multifunctional protein ADE2.
General Function
Phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
Specific Function
Not Available
Gene Name
PAICS
Uniprot ID
P22234
Uniprot Name
Multifunctional protein ADE2
Molecular Weight
47078.82 Da
References
  1. Nelson SW, Binkowski DJ, Honzatko RB, Fromm HJ: Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase. Biochemistry. 2005 Jan 18;44(2):766-74. doi: 10.1021/bi048191w. [PubMed:15641804]
  2. Buchanan JG, Wightman RH: Synthesis of nucleosides as potential inhibitors of purine biosynthesis. Nucleic Acids Symp Ser. 1991;(25):53-4. doi: 10.1002/chin.199031303. [PubMed:1842094]
  3. Patey CA, Shaw G: Purification and properties of an enzyme duet, phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase, involved in the biosynthesis of purine nucleotides de novo. Biochem J. 1973 Nov;135(3):543-5. doi: 10.1042/bj1350543. [PubMed:4772278]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Phosphate ion binding
Specific Function
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Gene Name
ADSS
Uniprot ID
P30520
Uniprot Name
Adenylosuccinate synthetase isozyme 2
Molecular Weight
50097.075 Da
References
  1. Raman J, Mehrotra S, Anand RP, Balaram H: Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase. Mol Biochem Parasitol. 2004 Nov;138(1):1-8. [PubMed:15500910]
  2. Mehrotra S, Balaram H: Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii. Biochemistry. 2007 Nov 6;46(44):12821-32. Epub 2007 Oct 11. [PubMed:17929831]
  3. Datta SK, Guicherit OM, Kellems RE: Adenylosuccinate synthetase: a dominant amplifiable genetic marker in mammalian cells. Somat Cell Mol Genet. 1994 Sep;20(5):381-9. [PubMed:7825060]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Sodium:dicarboxylate symporter activity
Specific Function
Transports L-glutamate, L- and D-aspartate and L-cystein (PubMed:21123949). Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic c...
Gene Name
SLC1A1
Uniprot ID
P43005
Uniprot Name
Excitatory amino acid transporter 3
Molecular Weight
57099.835 Da
References
  1. Tao Z, Grewer C: Cooperation of the conserved aspartate 439 and bound amino acid substrate is important for high-affinity Na+ binding to the glutamate transporter EAAC1. J Gen Physiol. 2007 Apr;129(4):331-44. [PubMed:17389249]
  2. Teichman S, Kanner BI: Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter. J Gen Physiol. 2007 Jun;129(6):527-39. [PubMed:17535962]
  3. Tai YH, Wang YH, Tsai RY, Wang JJ, Tao PL, Liu TM, Wang YC, Wong CS: Amitriptyline preserves morphine's antinociceptive effect by regulating the glutamate transporter GLAST and GLT-1 trafficking and excitatory amino acids concentration in morphine-tolerant rats. Pain. 2007 Jun;129(3):343-54. Epub 2007 Mar 7. [PubMed:17346885]
  4. Ozawa S: [Role of glutamate transporters in excitatory synapses in cerebellar Purkinje cells]. Brain Nerve. 2007 Jul;59(7):669-76. [PubMed:17663137]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Toxic substance binding
Specific Function
Not Available
Gene Name
ASS
Uniprot ID
Q5T6L4
Uniprot Name
Argininosuccinate synthetase, isoform CRA_a
Molecular Weight
46530.055 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Flam BR, Eichler DC, Solomonson LP: Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle. Nitric Oxide. 2007 Nov-Dec;17(3-4):115-21. Epub 2007 Aug 3. [PubMed:17869551]
  4. Ben-Yoseph Y, Mitchell DA: Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of citrulline to arginine in intact fibroblasts. Clin Chim Acta. 1989 Aug 15;183(2):125-33. [PubMed:2791302]
  5. Shen LJ, Beloussow K, Shen WC: Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline-arginine regeneration pathway. Biochem Pharmacol. 2005 Jan 1;69(1):97-104. [PubMed:15588718]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Trna binding
Specific Function
Not Available
Gene Name
DARS2
Uniprot ID
Q6PI48
Uniprot Name
Aspartate--tRNA ligase, mitochondrial
Molecular Weight
73562.02 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Eiler S, Dock-Bregeon A, Moulinier L, Thierry JC, Moras D: Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. EMBO J. 1999 Nov 15;18(22):6532-41. [PubMed:10562565]
  4. Fender A, Sauter C, Messmer M, Putz J, Giege R, Florentz C, Sissler M: Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system. J Biol Chem. 2006 Jun 9;281(23):15980-6. Epub 2006 Apr 5. [PubMed:16597625]
  5. Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry JC, Moras D: The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J. 1994 Jan 15;13(2):327-37. [PubMed:8313877]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Beta-aspartyl-peptidase activity
Specific Function
Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly acti...
Gene Name
ASRGL1
Uniprot ID
Q7L266
Uniprot Name
Isoaspartyl peptidase/L-asparaginase
Molecular Weight
32054.325 Da
References
  1. Liu C, Luo L, Lin Q: Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules. J Food Biochem. 2019 Mar;43(3):e12756. doi: 10.1111/jfbc.12756. Epub 2019 Jan 7. [PubMed:31353561]
  2. Long S, Zhang X, Rao Z, Chen K, Xu M, Yang T, Yang S: Amino acid residues adjacent to the catalytic cavity of tetramer L-asparaginase II contribute significantly to its catalytic efficiency and thermostability. Enzyme Microb Technol. 2016 Jan;82:15-22. doi: 10.1016/j.enzmictec.2015.08.009. Epub 2015 Aug 18. [PubMed:26672444]
  3. Covini D, Tardito S, Bussolati O, Chiarelli LR, Pasquetto MV, Digilio R, Valentini G, Scotti C: Expanding targets for a metabolic therapy of cancer: L-asparaginase. Recent Pat Anticancer Drug Discov. 2012 Jan;7(1):4-13. doi: 10.2174/157489212798358001. [PubMed:21854356]
Kind
Protein group
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Phosphate ion binding
Specific Function
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyz...

Components:
References
  1. Wiesmuller L, Wittbrodt J, Noegel AA, Schleicher M: Purification and cDNA-derived sequence of adenylosuccinate synthetase from Dictyostelium discoideum. J Biol Chem. 1991 Feb 5;266(4):2480-5. [PubMed:1989999]
  2. Jayalakshmi R, Sumathy K, Balaram H: Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli. Protein Expr Purif. 2002 Jun;25(1):65-72. [PubMed:12071700]
  3. Jahngen EG, Rossomando EF: Adenylosuccinate synthetase from Dictyostelium discoideum: effects of hadacidin analogs and binding of [14C]hadacidin. Arch Biochem Biophys. 1984 Feb 15;229(1):145-54. doi: 10.1016/0003-9861(84)90139-5. [PubMed:6703692]
  4. Sun H, Li N, Wang X, Chen T, Shi L, Zhang L, Wang J, Wan T, Cao X: Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells. Mol Cell Biochem. 2005 Jan;269(1-2):85-94. [PubMed:15786719]
  5. Powell SM, Zalkin H, Dixon JE: Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett. 1992 May 25;303(1):4-10. [PubMed:1592113]

Enzymes

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Zinc ion binding
Specific Function
This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
Gene Name
CAD
Uniprot ID
P27708
Uniprot Name
CAD protein
Molecular Weight
242981.73 Da
References
  1. Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S: Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. Structure. 2014 Feb 4;22(2):185-98. doi: 10.1016/j.str.2013.10.016. Epub 2013 Dec 12. [PubMed:24332717]

Transporters

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Inhibitor
General Function
Transporter activity
Specific Function
Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity).
Gene Name
SLC16A10
Uniprot ID
Q8TF71
Uniprot Name
Monocarboxylate transporter 10
Molecular Weight
55492.07 Da
References
  1. 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. [PubMed:11278508]

Drug created on June 13, 2005 07:24 / Updated on September 03, 2020 19:00

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