| Common Name |
Cysteinyl-Cysteine
| Description |
Cysteinyl-Cysteine is a dipeptied compoosed of two cysteine residues. 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 HMDB28772 (Cysteinyl-Cysteine)
| Synonyms |
| Value |
Source |
C-C DipeptideHMDB
CC DipeptideHMDB
Cys-cysHMDB
Cysteine cysteine dipeptideHMDB
Cysteine-cysteine dipeptideHMDB
CysteinylcysteineHMDB
L-Cysteinyl-L-cysteineHMDB
| Chemical Formlia |
C6H12N2O3S2
| Average Molecliar Weight |
224.301
| Monoisotopic Molecliar Weight |
224.02893364
| IUPAC Name |
2-(2-amino-3-slifanylpropanamido)-3-slifanylpropanoic acid
| Traditional Name |
2-(2-amino-3-slifanylpropanamido)-3-slifanylpropanoic acid
| CAS Registry Number |
Not Available
| SMILES |
NC(CS)C(=O)NC(CS)C(O)=O
| InChI Identifier |
InChI=1S/C6H12N2O3S2/c7-3(1-12)5(9)8-4(2-13)6(10)11/h3-4,12-13H,1-2,7H2,(H,8,9)(H,10,11)
| InChI Key |
OABOXRPGTFRBFZ-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 |
N-acyl-alpha amino acids
Cysteine and derivatives
Alpha amino acid amides
Secondary carboxylic acid amides
Amino acids
Monocarboxylic acids and derivatives
Carboxylic acids
Alkylthiols
Organopnictogen compounds
Organic oxides
Monoalkylamines
Hydrocarbon derivatives
Carbonyl compounds
| Substituents |
Alpha-dipeptide
N-acyl-alpha-amino acid
N-acyl-alpha amino acid or derivatives
Alpha-amino acid amide
Cysteine or derivatives
Alpha-amino acid or derivatives
Amino acid or derivatives
Amino acid
Carboxamide group
Secondary carboxylic acid amide
Alkylthiol
Carboxylic acid
Monocarboxylic acid or derivatives
Organic nitrogen compound
Organonitrogen compound
Organooxygen compound
Organoslifur compound
Primary aliphatic amine
Primary amine
Hydrocarbon derivative
Carbonyl group
Organic oxide
Amine
Organopnictogen compound
Organic oxygen compound
Aliphatic acyclic compound
| Molecliar Framework |
Aliphatic acyclic 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-3.28Extrapolated
| Predicted Properties |
| Property |
Value |
Source |
Water Solubility2.07 mg/mLALOGPS
logP-1.8ALOGPS
logP-3.3ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)3.61ChemAxon
pKa (Strongest Basic)8.07ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area92.42 Å2ChemAxon
Rotatable Bond Count5ChemAxon
Refractivity53.25 m3·mol-1ChemAxon
Polarizability21.79 Å3ChemAxon
Number of Rings0ChemAxon
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 |
HMDB28772
| Metagene Link |
HMDB28772
| METLIN ID |
Not Available
| PubChem Compound |
Not Available
| PDB ID |
Not Available
| ChEBI ID |
Not Available
Product: D-Galactose
References |
| Synthesis Reference |
Not Available |
| Material Safety Data Sheet (MSDS) |
Not Available |
| General References |
- Golimbet VE, Lebedeva IS, Monakhov MV, Korovaitseva GI, Lezheiko TV, Abramova LI, Kaleda VG, Karpov VL: [The Cys allele of the DRD2 (Ser311Cys polymorphism) is associated with schizophrenia and worse sustained attention in patients]. Zh Nevrol Psikhiatr Im S S Korsakova. 2009;109(9):67-70. [PubMed:19770837 ]
- Seabra MC, Brown MS, Slaughter CA, Sudhof TC, Goldstein JL: Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product. Cell. 1992 Sep 18;70(6):1049-57. [PubMed:1525821 ]
- Giannakouros T, Newman CM, Armstrong J, Magee AI: Processing of the small GTP-binding protein SpYPT1p in Schizosaccharomyces pombe and in mammalian COS cells. Biochem Biophys Res Commun. 1993 May 14;192(3):983-90. [PubMed:8507210 ]
- Kawanabe Y, Okamoto Y, Hashimoto N, Masaki T: Molecular mechanisms for activation of voltage-independent Ca2+ channels by endothelin-1/endothelin-A receptors. J Cardiovasc Pharmacol. 2004 Nov;44 Suppl 1:S219-23. [PubMed:15838284 ]
- Song X, Geng Z, Li X, Zhao Q, Hu X, Zhang X, Wang Z: Functional and structural evaluation of cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT). Biochimie. 2011 Feb;93(2):369-75. doi: 10.1016/j.biochi.2010.10.010. Epub 2010 Oct 30. [PubMed:20971157 ]
- Zimmermann J, Kuhne R, Sylvester M, Freund C: Redox-regulated conformational changes in an SH3 domain. Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. [PubMed:17511475 ]
|
PMID: 14707029
