Explore a selection of our essential drug information below, or:
Identification
- Generic Name
- 1-ACETYL-2-CARBOXYPIPERIDINE
- DrugBank Accession Number
- DB07384
- Background
Not Available
- Type
- Small Molecule
- Groups
- Experimental
- Structure
Structure for 1-ACETYL-2-CARBOXYPIPERIDINE (DB07384)
- Weight
- Average: 171.1937
Monoisotopic: 171.089543287 - Chemical Formula
- C8H13NO3
- Synonyms
- Not Available
Pharmacology
- Indication
Not Available
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.- Contraindications & Blackbox Warnings
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Not Available
- Mechanism of action
Target Actions Organism UATP synthase subunit alpha, mitochondrial Not Available Humans UATP synthase subunit beta, mitochondrial Not Available Humans UATP synthase subunit gamma, mitochondrial Not Available Humans - Absorption
Not Available
- 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
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
Not Available
- Pathways
- Not Available
- 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
- Not Available
Categories
- Drug Categories
- Not Available
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as n-acyl-l-alpha-amino acids. These are n-acylated 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
- N-acyl-L-alpha-amino acids
- Alternative Parents
- Piperidinecarboxylic acids / N-acylpiperidines / Tertiary carboxylic acid amides / Acetamides / Monocarboxylic acids and derivatives / Carboxylic acids / Azacyclic compounds / Organopnictogen compounds / Organonitrogen compounds / Organic oxides show 2 more
- Substituents
- Acetamide / Aliphatic heteromonocyclic compound / Azacycle / Carbonyl group / Carboxamide group / Carboxylic acid / Hydrocarbon derivative / Monocarboxylic acid or derivatives / N-acyl-l-alpha-amino acid / N-acyl-piperidine show 10 more
- Molecular Framework
- Aliphatic heteromonocyclic compounds
- External Descriptors
- N-acylpiperidine, piperidinemonocarboxylic acid (CHEBI:40797)
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- Not Available
- CAS number
- Not Available
- InChI Key
- JACZWLDAHFCGCC-ZETCQYMHSA-N
- InChI
- InChI=1S/C8H13NO3/c1-6(10)9-5-3-2-4-7(9)8(11)12/h7H,2-5H2,1H3,(H,11,12)/t7-/m0/s1
- IUPAC Name
- (2S)-1-acetylpiperidine-2-carboxylic acid
- SMILES
- [H][C@]1(CCCCN1C(C)=O)C(O)=O
References
- General References
- Not Available
- External Links
- PubChem Compound
- 5287692
- PubChem Substance
- 99443855
- ChemSpider
- 4450009
- ZINC
- ZINC000169386053
- PDBe Ligand
- APP
Clinical Trials
- Clinical Trials
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Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 303.0 mg/mL ALOGPS logP 0.16 ALOGPS logP -0.043 Chemaxon logS 0.25 ALOGPS pKa (Strongest Acidic) 4 Chemaxon pKa (Strongest Basic) -1.6 Chemaxon Physiological Charge -1 Chemaxon Hydrogen Acceptor Count 3 Chemaxon Hydrogen Donor Count 1 Chemaxon Polar Surface Area 57.61 Å2 Chemaxon Rotatable Bond Count 1 Chemaxon Refractivity 42.23 m3·mol-1 Chemaxon Polarizability 17.44 Å3 Chemaxon Number of Rings 1 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter Yes Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.9207 Blood Brain Barrier + 0.7649 Caco-2 permeable + 0.6506 P-glycoprotein substrate Non-substrate 0.5736 P-glycoprotein inhibitor I Non-inhibitor 0.8487 P-glycoprotein inhibitor II Non-inhibitor 0.972 Renal organic cation transporter Non-inhibitor 0.7352 CYP450 2C9 substrate Non-substrate 0.7792 CYP450 2D6 substrate Non-substrate 0.6809 CYP450 3A4 substrate Non-substrate 0.5461 CYP450 1A2 substrate Non-inhibitor 0.9084 CYP450 2C9 inhibitor Non-inhibitor 0.9288 CYP450 2D6 inhibitor Non-inhibitor 0.9675 CYP450 2C19 inhibitor Non-inhibitor 0.9131 CYP450 3A4 inhibitor Non-inhibitor 0.9715 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9772 Ames test Non AMES toxic 0.8217 Carcinogenicity Non-carcinogens 0.9666 Biodegradation Ready biodegradable 0.7715 Rat acute toxicity 1.8616 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9743 hERG inhibition (predictor II) Non-inhibitor 0.9613
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
Spectrum Spectrum Type Splash Key Predicted GC-MS Spectrum - GC-MS Predicted GC-MS splash10-0006-9300000000-925bd05a3dc12f5a6e60 Predicted MS/MS Spectrum - 10V, Positive (Annotated) Predicted LC-MS/MS splash10-003r-8900000000-19a54477f41927a8bad9 Predicted MS/MS Spectrum - 10V, Negative (Annotated) Predicted LC-MS/MS splash10-00b9-1900000000-81398f8cc5bd309a4ebb Predicted MS/MS Spectrum - 20V, Negative (Annotated) Predicted LC-MS/MS splash10-004i-4900000000-4158810af8be8d10ec20 Predicted MS/MS Spectrum - 20V, Positive (Annotated) Predicted LC-MS/MS splash10-003r-9500000000-b15f7fa79c75e58a0c0c Predicted MS/MS Spectrum - 40V, Negative (Annotated) Predicted LC-MS/MS splash10-0gz9-9600000000-ea476349c4a6c760e588 Predicted MS/MS Spectrum - 40V, Positive (Annotated) Predicted LC-MS/MS splash10-0059-9200000000-4c4ca541baba16600db5 Predicted 1H NMR Spectrum 1D NMR Not Applicable Predicted 13C NMR Spectrum 1D NMR Not Applicable - Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 129.67494 predictedDeepCCS 1.0 (2019) [M+H]+ 132.25417 predictedDeepCCS 1.0 (2019) [M+Na]+ 140.77338 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159)
- Specific Function
- Adp binding
- Gene Name
- ATP5F1A
- Uniprot ID
- P25705
- Uniprot Name
- ATP synthase subunit alpha, mitochondrial
- Molecular Weight
- 59750.06 Da
References
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits
- Specific Function
- Angiostatin binding
- Gene Name
- ATP5F1B
- Uniprot ID
- P06576
- Uniprot Name
- ATP synthase subunit beta, mitochondrial
- Molecular Weight
- 56559.42 Da
References
- 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. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits
- Specific Function
- Proton-transporting atp synthase activity, rotational mechanism
- Gene Name
- ATP5F1C
- Uniprot ID
- P36542
- Uniprot Name
- ATP synthase subunit gamma, mitochondrial
- Molecular Weight
- 32995.665 Da
References
- 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. [Article]
Drug created at September 15, 2010 21:21 / Updated at June 12, 2020 16:52