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Human Metabolome Database Version 2.5

 

Showing metabocard for Cinnavalininate (HMDB04078)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 11:24:21
Update Date 2009-05-05 20:59:59
Accession Number HMDB04078
Secondary Accession Numbers Not Available
Common Name Cinnavalininate
Description Cinnavalininate is an intermediate in the tryptophan metabolic pathway [Kegg: C05640]. It is generated from 3-hydroxyanthranilate via the enzyme catalase (EC:1.11.1.6).
Synonyms
  1. Cinnabarinic acid
  2. Cinnavalininic acid
  3. 2-Amino-3H-phenoxazin-one-1,9-dicarboxylic acid
  4. 2-Amino-3-oxo-3H-phenoxazin-1,9-dicarboxylic acid
Chemical IUPAC Name 2-amino-3-oxo-phenoxazine-1,9-dicarboxylic acid
Chemical Formula C14H8N2O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellanous
Class
  • Aminobenzoates
Sub Class
  • Miscellaneous heterocyclic compounds
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 300.223
Monoisotopic Molecular Weight 300.038239
Isomeric SMILES NC1=C(C(O)=O)C2=NC3=C(C=CC=C3OC2=CC1=O)C(O)=O
Canonical SMILES NC1=C(C(O)=O)C2=NC3=C(C=CC=C3OC2=CC1=O)C(O)=O
KEGG Compound ID C05640 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB04078 Link Image
Metagene Link HMDB04078 Link Image
METLIN ID Not Available
PubChem Compound 114918 Link Image
PubChem Substance 691858 Link Image
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C14H8N2O6/c15-10-6(17)4-8-12(9(10)14(20)21)16-11-5(13(18)19)2-1-3-7(11)22-8/h1-4H,15H2,(H,18,19)(H,20,21)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.146 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity 0.604 Source: PhysProp
Predicted LogP/Hydrophobicity 0.70 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References Not Available
Metabolic Enzymes
  1. Catalase
  2. cDNA FLJ78138, highly similar to Homo sapiens catalase
Enzyme 1 [top]
Enzyme 1 ID 6878
Enzyme 1 Name Catalase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name CAT
Enzyme 1 Protein Sequence >Catalase 
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme 1 Number of Residues 527
Enzyme 1 Molecular Weight 59757
Enzyme 1 Theoretical pI 7.41
Enzyme 1 GO Classification
Function
  • antioxidant activity
  • catalase activity
  • peroxidase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 1 General Function Inorganic ion transport and metabolism
Enzyme 1 Specific Function Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 2 H2O2 = O2 + 2 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1228085 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P04040 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CATA_HUMAN Link Image
Enzyme 1 PDB ID 1F4J Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >66 bp 
ATGGCTGACAGCCGGGATCCCGCCAGCGACCAGATGCAGCACTGGAAGGAGCAGCGGGCC
GCGCAG
Enzyme 1 GenBank Gene ID X04085 Link Image
Enzyme 1 GeneCard ID CAT Link Image
Enzyme 1 GenAtlas ID CAT Link Image
Enzyme 1 HGNC ID HGNC:1516 Link Image
Enzyme 1 Chromosome Location 11
Enzyme 1 Locus 11p13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Quan F, Korneluk RG, Tropak MB, Gravel RA: Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986 Jul 11;14(13):5321-35. [PubMed Link Image]
  2. Bell GI, Najarian RC, Mullenbach GT, Hallewell RA: cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561-2. [PubMed Link Image]
  3. Jin LH, Bahn JH, Eum WS, Kwon HY, Jang SH, Han KH, Kang TC, Won MH, Kang JH, Cho SW, Park J, Choi SY: Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic Biol Med. 2001 Dec 1;31(11):1509-19. [PubMed Link Image]
  4. Yoo JH, Erzurum SC, Hay JG, Lemarchand P, Crystal RG: Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. J Clin Invest. 1994 Jan;93(1):297-302. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819-23. [PubMed Link Image]
  7. Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ: Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. [PubMed Link Image]
  8. Putnam CD, Arvai AS, Bourne Y, Tainer JA: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. [PubMed Link Image]
  9. Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP: Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13119
Enzyme 2 Name cDNA FLJ78138, highly similar to Homo sapiens catalase
Enzyme 2 Synonyms
  1. CAT, mRNA
  2. Catalase, isoform CRA_a
Enzyme 2 Gene Name CAT
Enzyme 2 Protein Sequence >cDNA FLJ78138, highly similar to Homo sapiens catalase 
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme 2 Number of Residues 527
Enzyme 2 Molecular Weight 59757
Enzyme 2 Theoretical pI 7.41
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Inorganic ion transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158256602 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8K6C0 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8K6C0_HUMAN Link Image
Enzyme 2 PDB ID 1F4J Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AK291585 Link Image
Enzyme 2 GeneCard ID A8K6C0 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available