Valyl-Isoleucine Description
Valyl-Isoleucine is a dipeptide composed of valine and isoleucine. 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 HMDB29130 (Valyl-Isoleucine)
Synonyms
Value Source L-Valyl-L-isoleucineHMDB V-I dipeptideHMDB Val-ileHMDB Valine isoleucine dipeptideHMDB Valine-isoleucine dipeptideHMDB ValylisoleucineHMDB VI dipeptideHMDB
Chemical Formlia
C11H22N2O3 Average Molecliar Weight
230.304 Monoisotopic Molecliar Weight
230.16304258 IUPAC Name
2-(2-amino-3-methylbutanamido)-3-methylpentanoic acid Traditional Name
2-(2-amino-3-methylbutanamido)-3-methylpentanoic acid CAS Registry Number
Not Available SMILES
InChI Identifier
InChI Key
PNVLWFYAPWAQMU-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-1.16Extrapolated
Predicted Properties
Property Value Source Water Solubility10.9 mg/mLALOGPS logP-1.1ALOGPS logP-1.2ChemAxon logS-1.3ALOGPS pKa (Strongest Acidic)4.06ChemAxon pKa (Strongest Basic)8.51ChemAxon Physiological Charge0ChemAxon Hydrogen Acceptor Count4ChemAxon Hydrogen Donor Count3ChemAxon Polar Surface Area92.42 Å2ChemAxon Rotatable Bond Count6ChemAxon Refractivity60.39 m3·mol-1ChemAxon Polarizability25.27 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
HMDB29130 Metagene Link
HMDB29130 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- Yang S, Jia C, Zhu H, Han S: CYP1A1 Ile462Val polymorphism and cervical cancer: evidence from a meta-analysis. Tumour Biol. 2012 Dec;33(6):2265-72. doi: 10.1007/s13277-012-0488-y. Epub 2012 Sep 5. [PubMed:22948778 ]
- Yeaman SJ, Cohen P, Watson DC, Dixon GH: The substrate specificity of adenosine 3:5-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle. Biochem J. 1977 Feb 15;162(2):411-21. [PubMed:192223 ]
- Hirsch-Behnam A, Delius H, de Villiers EM: A comparative sequence analysis of two human papillomavirus (HPV) types 2a and 57. Virus Res. 1990 Dec;18(1):81-97. [PubMed:1964523 ]