| Common Name |
Prolyl-Cysteine
| Description |
Prolyl-Cysteine is a dipeptide composed of proline and cysteine. It is an incomplete breakdown product of protein digestion or protein catabolism. Some dipeptides are known to have physiological or cell-signaling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis. This dipeptide has not yet been identified in human tissues or biofluids and so it is classified as an Expected metabolite.
| Structure |
MOLSDF3D-SDFPDBSMILESInChI View 3D Structure
Structure for HMDB29014 (Prolyl-Cysteine)
| Synonyms |
| Value |
Source |
L-Prolyl-L-cysteineHMDB
P-C DipeptideHMDB
PC DipeptideHMDB
pro-CysHMDB
Proline cysteine dipeptideHMDB
Proline-cysteine dipeptideHMDB
ProlylcysteineHMDB
| Chemical Formlia |
C8H14N2O3S
| Average Molecliar Weight |
218.273
| Monoisotopic Molecliar Weight |
218.072513014
| IUPAC Name |
2-(pyrrolidin-2-ylformamido)-3-slifanylpropanoic acid
| Traditional Name |
2-(pyrrolidin-2-ylformamido)-3-slifanylpropanoic acid
| CAS Registry Number |
Not Available
| SMILES |
OC(=O)C(CS)NC(=O)C1CCCN1
| InChI Identifier |
InChI=1S/C8H14N2O3S/c11-7(5-2-1-3-9-5)10-6(4-14)8(12)13/h5-6,9,14H,1-4H2,(H,10,11)(H,12,13)
| InChI Key |
HXNYBZQLBWIADP-UHFFFAOYSA-N
| Chemical Taxonomy |
| Description |
This compound belongs to the class of chemical entities known as dipeptides. These are organic compounds containing a sequence of exactly two alpha-amino acids joined by a peptide bond.
| Kingdom |
Chemical entities
| Super Class |
Organic compounds
| Class |
Organic acids and derivatives
| Sub Class |
Carboxylic acids and derivatives
| Direct Parent |
Dipeptides
| Alternative Parents |
Proline and derivatives
N-acyl-alpha amino acids
Alpha amino acid amides
Cysteine and derivatives
Pyrrolidinecarboxamides
Secondary carboxylic acid amides
Amino acids
Alkylthiols
Monocarboxylic acids and derivatives
Dialkylamines
Carboxylic acids
Azacyclic compounds
Carbonyl compounds
Hydrocarbon derivatives
Organic oxides
Organopnictogen compounds
| Substituents |
Alpha-dipeptide
N-acyl-alpha-amino acid
N-acyl-alpha amino acid or derivatives
Proline or derivatives
Alpha-amino acid amide
Cysteine or derivatives
Alpha-amino acid or derivatives
Pyrrolidine carboxylic acid or derivatives
Pyrrolidine-2-carboxamide
Pyrrolidine
Amino acid or derivatives
Carboxamide group
Amino acid
Secondary carboxylic acid amide
Organoheterocyclic compound
Secondary amine
Azacycle
Alkylthiol
Carboxylic acid
Secondary aliphatic amine
Monocarboxylic acid or derivatives
Hydrocarbon derivative
Organopnictogen compound
Organic oxide
Organonitrogen compound
Organooxygen compound
Carbonyl group
Amine
Organoslifur compound
Organic nitrogen compound
Organic oxygen compound
Aliphatic heteromonocyclic compound
| Molecliar Framework |
Aliphatic heteromonocyclic compounds
| External Descriptors |
Not Available
| Ontology |
| Status |
Expected but not Quantified
| Origin |
Endogenous
| Biofunction |
Not Available
| Application |
Not Available
| Cellliar locations |
Not Available
| Physical Properties |
| State |
Solid
| Experimental Properties |
| Property |
Value |
Reference |
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogP-3.06Extrapolated
| Predicted Properties |
| Property |
Value |
Source |
Water Solubility1.9 mg/mLALOGPS
logP-0.74ALOGPS
logP-3.1ChemAxon
logS-2.1ALOGPS
pKa (Strongest Acidic)3.64ChemAxon
pKa (Strongest Basic)9.61ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area78.43 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity53.09 m3·mol-1ChemAxon
Polarizability21.87 Å3ChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rlie of FiveYesChemAxon
Ghose FilterYesChemAxon
Vebers RlieYesChemAxon
MDDR-like RlieYesChemAxon
| Spectra |
| Spectra |
Not Available
| Biological Properties |
| Cellliar Locations |
Not Available
| Biofluid Locations |
Not Available
| Tissue Location |
Not Available
| Pathways |
Not Available
| Normal Concentrations |
| Not Available |
| Abnormal Concentrations |
|
Not Available
| Associated Disorders and Diseases |
| Disease References |
None
| Associated OMIM IDs |
None
| External Links |
| DrugBank ID |
Not Available
| DrugBank Metabolite ID |
Not Available
| Phenol Explorer Compound ID |
Not Available
| Phenol Explorer Metabolite ID |
Not Available
| FoodDB ID |
Not Available
| KNApSAcK ID |
Not Available
| Chemspider ID |
Not Available
| KEGG Compound ID |
Not Available
| BioCyc ID |
Not Available
| BiGG ID |
Not Available
| Wikipedia Link |
Not Available
| NuGOwiki Link |
HMDB29014
| Metagene Link |
HMDB29014
| METLIN ID |
Not Available
| PubChem Compound |
Not Available
| PDB ID |
Not Available
| ChEBI ID |
Not Available
Product: COH29
References |
| Synthesis Reference |
Not Available |
| Material Safety Data Sheet (MSDS) |
Not Available |
| General References |
- Dong A, Yoder JA, Zhang X, Zhou L, Bestor TH, Cheng X: Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 2001 Jan 15;29(2):439-48. [PubMed:11139614 ]
- Liu Y, Santi DV: m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8263-5. [PubMed:10899996 ]
- Yarus M: Perspectives: protein synthesis. Unraveling the riddle of ProCys tRNA synthetase. Science. 2000 Jan 21;287(5452):440-1. [PubMed:10671174 ]
- Kossykh VG, Schlagman SL, Hattman S: Function of Pro-185 in the ProCys of conserved motif IV in the EcoRII [cytosine-C5]-DNA methyltransferase. FEBS Lett. 1995 Aug 14;370(1-2):75-7. [PubMed:7649307 ]
|
PMID: 7846211
