Serinyl-Arginine Description
Serinyl-Arginine is a dipeptide composed of serine 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
Structure for HMDB29033 (Serinyl-Arginine)
Synonyms
Value Source L-Serinyl-L-arginineHMDB S-R DipeptideHMDB Ser-argHMDB Serine arginine dipeptideHMDB Serine-arginine dipeptideHMDB SerinylarginineHMDB SR DipeptideHMDB
Chemical Formlia
C9H19N5O4 Average Molecliar Weight
261.2783 Monoisotopic Molecliar Weight
261.143704121 IUPAC Name
2-(2-amino-3-hydroxypropanamido)-5-carbamimidamidopentanoic acid Traditional Name
2-(2-amino-3-hydroxypropanamido)-5-carbamimidamidopentanoic acid CAS Registry Number
Not Available SMILES
InChI Identifier
InChI Key
RZEQTVHJZCIUBT-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
Substituents
Molecliar Framework
Aliphatic acyclic compounds External Descriptors
Not Available Ontology Status
Expected but not Quantified Origin
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-4.73Extrapolated
Predicted Properties
Property Value Source Water Solubility1.03 mg/mLALOGPS logP-3.8ALOGPS logP-4.7ChemAxon logS-2.4ALOGPS pKa (Strongest Acidic)3.53ChemAxon pKa (Strongest Basic)12.06ChemAxon Physiological Charge1ChemAxon Hydrogen Acceptor Count8ChemAxon Hydrogen Donor Count7ChemAxon Polar Surface Area174.55 Å2ChemAxon Rotatable Bond Count8ChemAxon Refractivity72.76 m3·mol-1ChemAxon Polarizability26.32 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
HMDB29033 Metagene Link
HMDB29033 METLIN ID
Not Available PubChem Compound
Not Available PDB ID
Not Available ChEBI ID
Not Available
References Synthesis Reference Not Available Material Safety Data Sheet (MSDS) Not Available General References- Kim E, Du L, Bregman DB, Warren SL: Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA. J Cell Biol. 1997 Jan 13;136(1):19-28. [PubMed:9008700 ]
- Du L, Warren SL: A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing. J Cell Biol. 1997 Jan 13;136(1):5-18. [PubMed:9008699 ]