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Tryptophyl-Lysine

July 21, 2017
Common Name

Tryptophyl-Lysine Description

Tryptophyl-Lysine is a dipeptide composed of tryptophan and lysine. 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 HMDB29088 (Tryptophyl-Lysine)

Synonyms

Value Source L-Tryptophyl-L-lysineHMDB TRP-LysHMDB Tryptophan lysine dipeptideHMDB Tryptophan-lysine dipeptideHMDB TryptophyllysineHMDB W-K DipeptideHMDB WK DipeptideHMDB

Chemical Formlia

C17H24N4O3 Average Molecliar Weight

332.3975 Monoisotopic Molecliar Weight

332.184840654 IUPAC Name

6-amino-2-[2-amino-3-(1H-indol-3-yl)propanamido]hexanoic acid Traditional Name

6-amino-2-[2-amino-3-(1H-indol-3-yl)propanamido]hexanoic acid CAS Registry Number

Not Available SMILES

NCCCCC(NC(=O)C(N)CC1=CNC2=C1C=CC=C2)C(O)=O

InChI Identifier

InChI=1S/C17H24N4O3/c18-8-4-3-7-15(17(23)24)21-16(22)13(19)9-11-10-20-14-6-2-1-5-12(11)14/h1-2,5-6,10,13,15,20H,3-4,7-9,18-19H2,(H,21,22)(H,23,24)

InChI Key

DZHDVYLBNKMLMB-UHFFFAOYSA-N Chemical Taxonomy Classification

Not classified 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-1.88Extrapolated

    Predicted Properties

    Property Value Source Water Solubility0.36 mg/mLALOGPS logP-1.2ALOGPS logP-1.8ChemAxon logS-3ALOGPS pKa (Strongest Acidic)3.79ChemAxon pKa (Strongest Basic)10.21ChemAxon Physiological Charge1ChemAxon Hydrogen Acceptor Count5ChemAxon Hydrogen Donor Count5ChemAxon Polar Surface Area134.23 Å2ChemAxon Rotatable Bond Count9ChemAxon Refractivity90.81 m3·mol-1ChemAxon Polarizability35.57 Å3ChemAxon Number of Rings2ChemAxon 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

    HMDB29088 Metagene Link

    HMDB29088 METLIN ID

    Not Available PubChem Compound

    Not Available PDB ID

    Not Available ChEBI ID

    Not Available

    Product: Oleanolic acid derivative 2

    References Synthesis Reference Not Available Material Safety Data Sheet (MSDS) Not Available General References
    1. Joshi S, Ghosh I, Pokhrel S, Madler L, Nau WM: Interactions of amino acids and polypeptides with metal oxide nanoparticles probed by fluorescent indicator adsorption and displacement. ACS Nano. 2012 Jun 26;6(6):5668-79. doi: 10.1021/nn301669t. Epub 2012 May 22. [PubMed:22591378 ]
    2. Shine NR, James TL: Interactions of diastereomeric tripeptides of lysyl-5-fluorotryptophyllysine with DNA. 1. Optical and 19F NMR studies of native DNA complexes. Biochemistry. 1985 Jul 30;24(16):4333-41. [PubMed:4052400 ]
    3. Shine NR, Bubienko E, James TL: Interactions of diastereomeric tripeptides of lysyl-5-fluorotryptophyllysine with DNA. 2. Optical, 19F NMR, and strand cleavage studies of apurinic DNA complexes. Biochemistry. 1985 Jul 30;24(16):4341-5. [PubMed:4052401 ]
    4. Job GE, Kennedy RJ, Heitmann B, Miller JS, Walker SM, Kemp DS: Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards. J Am Chem Soc. 2006 Jun 28;128(25):8227-33. [PubMed:16787087 ]

    PMID: 11050288

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