| Common Name |
Glycyl-Arginine
| Description |
Glycyl-Arginine is a dipeptide composed of glycine and arginine. 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 HMDB28835 (Glycyl-Arginine)
| Synonyms |
| Value |
Source |
g-R DipeptideHMDB
Gly-argHMDB
Glycine arginine dipeptideHMDB
Glycine-arginine dipeptideHMDB
GlycylarginineHMDB
GR DipeptideHMDB
L-Glycyl-L-arginineHMDB
| Chemical Formlia |
C8H17N5O3
| Average Molecliar Weight |
231.2523
| Monoisotopic Molecliar Weight |
231.133139435
| IUPAC Name |
2-(2-aminoacetamido)-5-carbamimidamidopentanoic acid
| Traditional Name |
2-(2-aminoacetamido)-5-carbamimidamidopentanoic acid
| CAS Registry Number |
Not Available
| SMILES |
NCC(=O)NC(CCCNC(N)=N)C(O)=O
| InChI Identifier |
InChI=1S/C8H17N5O3/c9-4-6(14)13-5(7(15)16)2-1-3-12-8(10)11/h5H,1-4,9H2,(H,13,14)(H,15,16)(H4,10,11,12)
| InChI Key |
JLXVRFDTDUGQEE-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
Alpha amino acid amides
Fatty acids and conjugates
Secondary carboxylic acid amides
Guanidines
Amino acids
Propargyl-type 1,3-dipolar organic compounds
Monocarboxylic acids and derivatives
Carboxylic acids
Carboximidamides
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
Alpha-amino acid or derivatives
Fatty acid
Amino acid or derivatives
Carboxamide group
Amino acid
Secondary carboxylic acid amide
Guanidine
Carboxylic acid
Organic 1,3-dipolar compound
Propargyl-type 1,3-dipolar organic compound
Carboximidamide
Monocarboxylic acid or derivatives
Organic nitrogen compound
Organonitrogen compound
Organooxygen compound
Primary aliphatic amine
Primary amine
Hydrocarbon derivative
Organic oxide
Carbonyl group
Organopnictogen compound
Amine
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-4.25Extrapolated
| Predicted Properties |
| Property |
Value |
Source |
Water Solubility1.01 mg/mLALOGPS
logP-3.8ALOGPS
logP-4.2ChemAxon
logS-2.4ALOGPS
pKa (Strongest Acidic)3.6ChemAxon
pKa (Strongest Basic)12.18ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count7ChemAxon
Hydrogen Donor Count6ChemAxon
Polar Surface Area154.32 Å2ChemAxon
Rotatable Bond Count7ChemAxon
Refractivity66.73 m3·mol-1ChemAxon
Polarizability23.4 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 |
HMDB28835
| Metagene Link |
HMDB28835
| METLIN ID |
Not Available
| PubChem Compound |
Not Available
| PDB ID |
Not Available
| ChEBI ID |
Not Available
Product: Vanilpyruvic acid
References |
| Synthesis Reference |
Not Available |
| Material Safety Data Sheet (MSDS) |
Not Available |
| General References |
- Prell JS, Demireva M, Oomens J, Williams ER: Role of sequence in salt-bridge formation for alkali metal cationized GlyArg and ArgGly investigated with IRMPD spectroscopy and theory. J Am Chem Soc. 2009 Jan 28;131(3):1232-42. doi: 10.1021/ja808177z. [PubMed:19117387 ]
- Wallace RJ, McKain N, Broderick GA, Rode LM, Walker ND, Newbold CJ, Kopecny J: Peptidases of the rumen bacterium, Prevotella ruminicola. Anaerobe. 1997 Feb;3(1):35-42. [PubMed:16887560 ]
- Lacourse KA, Friis-Hansen L, Samuelson LC, Rehfeld JF: Altered processing of procholecystokinin in carboxypeptidase E-deficient fat mice: differential synthesis in neurons and endocrine cells. FEBS Lett. 1998 Sep 25;436(1):61-6. [PubMed:9771894 ]
- Wallace RJ, McKain N: A survey of peptidase activity in rumen bacteria. J Gen Microbiol. 1991 Sep;137(9):2259-64. [PubMed:1748877 ]
- Bleakman A, Smyth DG: Sequential processing reactions in the formation of hormone amides. Eur J Biochem. 1987 Aug 17;167(1):161-5. [PubMed:3113947 ]
- Roche PC, Ryan RJ: Electrophoretic analysis of membrane proteases in the luteinized rat ovary. Endocrinology. 1986 Aug;119(2):495-501. [PubMed:3525119 ]
- McKain N, Wallace RJ, Watt ND: Selective isolation of bacteria with dipeptidyl aminopeptidase type I activity from the sheep rumen. FEMS Microbiol Lett. 1992 Aug 15;74(2-3):169-73. [PubMed:1526449 ]
- Ishiura S, Anraku H, Kamo I, Koizumi H, Arahata K, Sugita H: Isolation of a Ca-dependent erythrolytic protein (perforin) from cytotoxic T-lymphocytes. J Biochem. 1987 Jul;102(1):9-12. [PubMed:3499435 ]
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PMID: 19649285