Posted inUncategorized

Cysteinyl-Histidine

July 21, 2017
Common Name

Cysteinyl-Histidine Description

Cysteinyl-Histidine is a dipeptide composed of cysteine and histidine. 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 HMDB28777 (Cysteinyl-Histidine)

Synonyms

Value Source C-H DipeptideHMDB CH DipeptideHMDB Cys-hisHMDB Cysteine histidine dipeptideHMDB Cysteine-histidine dipeptideHMDB CysteinylhistidineHMDB L-Cysteinyl-L-histidineHMDB

Chemical Formlia

C9H14N4O3S Average Molecliar Weight

258.297 Monoisotopic Molecliar Weight

258.078661024 IUPAC Name

2-(2-amino-3-slifanylpropanamido)-3-(1H-imidazol-5-yl)propanoic acid Traditional Name

2-(2-amino-3-slifanylpropanamido)-3-(3H-imidazol-4-yl)propanoic acid CAS Registry Number

Not Available SMILES

NC(CS)C(=O)NC(CC1=CN=CN1)C(O)=O

InChI Identifier

InChI=1S/C9H14N4O3S/c10-6(3-17)8(14)13-7(9(15)16)1-5-2-11-4-12-5/h2,4,6-7,17H,1,3,10H2,(H,11,12)(H,13,14)(H,15,16)

InChI Key

LVNMAAGSAUGNIC-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

  • Histidine and derivatives
  • N-acyl-alpha amino acids
  • Alpha amino acid amides
  • Cysteine and derivatives
  • Imidazolyl carboxylic acids and derivatives
  • Heteroaromatic compounds
  • Secondary carboxylic acid amides
  • Amino acids
  • Alkylthiols
  • Azacyclic compounds
  • Carboxylic acids
  • Monocarboxylic acids and derivatives
  • Carbonyl compounds
  • Organic oxides
  • Organopnictogen compounds
  • Monoalkylamines
  • Hydrocarbon derivatives

    • Substituents

  • Alpha-dipeptide
  • Histidine or derivatives
  • N-acyl-alpha-amino acid
  • N-acyl-alpha amino acid or derivatives
  • Alpha-amino acid amide
  • Cysteine or derivatives
  • Alpha-amino acid or derivatives
  • Imidazolyl carboxylic acid derivative
  • Azole
  • Heteroaromatic compound
  • Imidazole
  • Amino acid or derivatives
  • Amino acid
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Azacycle
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Alkylthiol
  • Organoheterocyclic compound
  • Organic nitrogen compound
  • Primary aliphatic amine
  • Organonitrogen compound
  • Organooxygen compound
  • Organoslifur compound
  • Primary amine
  • Carbonyl group
  • Hydrocarbon derivative
  • Organic oxide
  • Amine
  • Organopnictogen compound
  • Organic oxygen compound
  • Aromatic heteromonocyclic compound

    • Molecliar Framework

    Aromatic heteromonocyclic 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-3.87Extrapolated

    Predicted Properties

    Property Value Source Water Solubility0.58 mg/mLALOGPS logP-2.4ALOGPS logP-3.9ChemAxon logS-2.6ALOGPS pKa (Strongest Acidic)3.35ChemAxon pKa (Strongest Basic)8.09ChemAxon Physiological Charge0ChemAxon Hydrogen Acceptor Count5ChemAxon Hydrogen Donor Count5ChemAxon Polar Surface Area121.1 Å2ChemAxon Rotatable Bond Count6ChemAxon Refractivity63.08 m3·mol-1ChemAxon Polarizability25.26 Å3ChemAxon Number of Rings1ChemAxon 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

    HMDB28777 Metagene Link

    HMDB28777 METLIN ID

    Not Available PubChem Compound

    Not Available PDB ID

    Not Available ChEBI ID

    Not Available

    Product: Kinetin riboside

    References Synthesis Reference Not Available Material Safety Data Sheet (MSDS) Not Available General References
    1. Lockwood TD: The transfer of reductive energy and pace of proteome turnover: a theory of integrated catabolic control. Antioxid Redox Signal. 2005 Jul-Aug;7(7-8):982-98. [PubMed:15998253 ]
    2. Negi S, Itazu M, Imanishi M, Nomura A, Sugiura Y: Creation and characteristics of unnatural CysHis(3)-type zinc finger protein. Biochem Biophys Res Commun. 2004 Dec 10;325(2):421-5. [PubMed:15530409 ]
    3. Hirabayashi K, Hanaoka K, Shimonishi M, Terai T, Komatsu T, Ueno T, Nagano T: Selective two-step labeling of proteins with an off/on fluorescent probe. Chemistry. 2011 Dec 23;17(52):14763-71. doi: 10.1002/chem.201102664. Epub 2011 Nov 22. [PubMed:22106092 ]
    4. Laplaza CE, Holm RH: Stability and nickel binding properties of peptides designed as scaffolds for the stabilization of Ni(II)-Fe(4)S(4) bridged assemblies. J Biol Inorg Chem. 2002 Apr;7(4-5):451-60. Epub 2002 Jan 8. [PubMed:11941503 ]
    5. Lockwood TD: Is dihydrolipoic acid among the reductive activators of parasite CysHis proteases? Exp Parasitol. 2008 Apr;118(4):604-13. Epub 2007 Nov 7. [PubMed:18068706 ]
    6. Lockwood TD: Lysosomal metal, redox and proton cycles influencing the CysHis cathepsin reaction. Metallomics. 2013 Feb;5(2):110-24. doi: 10.1039/c2mt20156a. [PubMed:23302864 ]
    7. Lockwood TD: Responsiveness of parasite Cys His proteases to iron redox. Parasitol Res. 2006 Dec;100(1):175-81. Epub 2006 Jul 6. [PubMed:16823592 ]

    PMID: 1981582

    Last updated on