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Human Metabolome Database Version 2.5

 

Showing metabocard for Maleylacetoacetic acid (HMDB02052)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:34
Update Date 2009-11-25 04:01:02
Accession Number HMDB02052
Secondary Accession Numbers Not Available
Common Name Maleylacetoacetic acid
Description 4-Maleylacetoacetate is an intermediate in the metabolism of tyrosine. Homogentisate 1,2-dioxygenase is the enzyme, which catalyzes the conversion of homogentisate to 4-maleylacetoacetate. Homogentisate 1,2-dioxygenase or HGD is involved in the catabolism of aromatic rings, more specifically in the break down of the amino acids tyrosine and phenylalanine.
Synonyms
  1. Maleylacetoacetate
  2. 4-Maleylacetoacetic acid
  3. 4-Maleylacetoacetate
Chemical IUPAC Name (2Z)4,6-dioxooct-2-enedioic acid
Chemical Formula C8H8O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Dicarboxylic Acids
  • Keto-Acids
Sub Class
  • Long chain dicarboxylic acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • carboxylic acid
  • alkene
Biofunction
  • Component of Tyrosine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 200.145
Monoisotopic Molecular Weight 200.032089
Isomeric SMILES OC(=O)CC(=O)CC(=O)C=C/C(O)=O
Canonical SMILES OC(=O)CC(=O)CC(=O)C=CC(O)=O
KEGG Compound ID C01036 Link Image
BioCyc ID 4-MALEYL-ACETOACETATE Link Image
BiGG ID 1485279 Link Image
Wikipedia Link Maleylacetoacetate Link Image
NuGOwiki Link HMDB02052 Link Image
Metagene Link HMDB02052 Link Image
METLIN ID 6462 Link Image
PubChem Compound 5280393 Link Image
PubChem Substance 2031 Link Image
ChEBI ID 47904 Link Image
CAS Registry Number 5698-52-2
InChI Identifier InChI=1/C8H8O6/c9-5(1-2-7(11)12)3-6(10)4-8(13)14/h1-2H,3-4H2,(H,11,12)(H,13,14)/b2-1-
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.65 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.19 [Predicted by ALOGPS]; -0.4 [Predicted by PubChem via XLOGP] 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
  • Cytoplasm (Predicted from LogP)
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
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Kvittingen EA, Halvorsen S, Jellum E: Deficient fumarylacetoacetate fumarylhydrolase activity in lymphocytes and fibroblasts from patients with hereditary tyrosinemia. Pediatr Res. 1983 Jul;17(7):541-4. [PubMed Link Image]
  2. Gray RG, Patrick AD, Preston FE, Whitfield MF: Acute hereditary tyrosinaemia type I: clinical, biochemical and haematological studies in twins. J Inherit Metab Dis. 1981;4(1):37-40. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Homogentisate 1,2-dioxygenase
  2. Uncharacterized protein GSTZ1
Enzyme 1 [top]
Enzyme 1 ID 6123
Enzyme 1 Name Homogentisate 1,2-dioxygenase
Enzyme 1 Synonyms
  1. Homogentisicase
  2. Homogentisate oxygenase
  3. Homogentisic acid oxidase
Enzyme 1 Gene Name HGD
Enzyme 1 Protein Sequence >Homogentisate 1,2-dioxygenase 
MAELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFTCPRSTNKRSW
LYRILPSVSHKPFESIDEGHVTHNWDEVDPDPNQLRWKPFEIPKASQKKVDFVSGLHTLC
GAGDIKSNNGLAIHIFLCNTSMENRCFYNSDGDFLIVPQKGNLLIYTEFGKMLVQPNEIC
VIQRGMRFSIDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVP
GGYTVINKYQGKLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTV
LTAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGHYEAKQGGFLPG
GGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMFESSLSLAVTKWGLKASRCLD
ENYHKCWEPLKSHFTPNSRNPAEPN
Enzyme 1 Number of Residues 445
Enzyme 1 Molecular Weight 49973
Enzyme 1 Theoretical pI 7.00
Enzyme 1 GO Classification
Function
  • catalytic activity
  • homogentisate 1,2-dioxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Process
  • L-phenylalanine catabolism
  • L-phenylalanine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • tyrosine metabolism
Component
—
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Homogentisate + O(2) = 4-maleylacetoacetate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • homogentisate + O2 = 4-maleylacetoacetate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1616743 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q93099 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HGD_HUMAN Link Image
Enzyme 1 PDB ID 1EYB Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1338 bp 
ATGGCTGAGTTAAAGTACATTTCTGGATTTGGGAATGAGTGTTCTTCAGAGGATCCTCGC
TGCCCAGGTTCCCTGCCAGAAGGACAGAATAATCCTCAGGTCTGCCCCTACAATCTCTAT
GCTGAGCAGCTCTCAGGATCGGCTTTCACTTGTCCACGGAGCACCAATAAGAGAAGCTGG
CTGTATAGGATTCTACCTTCAGTTTCTCACAAGCCCTTTGAATCCATTGACGAAGGCCAT
GTCACTCACAACTGGGATGAAGTTGATCCTGATCCTAACCAGCTTAGATGGAAACCATTT
GAGATTCCAAAAGCATCTCAGAAGAAAGTAGACTTTGTGAGTGGCCTGCATACCTTGTGT
GGAGCTGGAGACATAAAGTCTAACAATGGGCTTGCTATCCACATTTTCCTCTGCAATACC
TCCATGGAGAACAGATGCTTTTACAATTCAGATGGGGACTTCTTGATTGTTCCGCAGAAA
GGGAACCTTCTCATTTACACCGAGTTTGGCAAGATGCTTGTACAGCCCAATGAGATCTGC
GTCATTCAGAGAGGAATGCGGTTCAGCATAGATGTCTTTGAGGAGACCAGGGGCTACATC
TTGGAGGTCTATGGTGTCCACTTTGAGTTACCTGACCTTGGACCAATTGGGGCCAATGGC
TTGGCCAATCCTCGTGATTTCTTGATACCCATTGCCTGGTATGAGGATCGCCAAGTACCA
GGTGGTTACACGGTCATTAATAAATACCAGGGCAAGCTGTTTGCTGCCAAACAGGATGTC
TCCCCGTTCAATGTTGTGGCCTGGCACGGGAATTATACACCCTACAAGTACAACCTGAAG
AATTTCATGGTTATCAACTCAGTGGCCTTTGACCATGCAGACCCATCCATTTTCACAGTA
TTGACTGCTAAGTCTGTCCGCCCTGGAGTGGCCATTGCTGATTTTGTCATCTTCCCACCT
CGATGGGGGGTTGCTGATAAGACCTTCAGGCCTCCTTATTACCATAGGAACTGCATGAGT
GAGTTCATGGGACTCATCCGAGGTCACTATGAGGCAAAGCAAGGTGGGTTCCTGCCAGGG
GGAGGGAGTCTACACAGCACAATGACCCCCCATGGACCTGATGCTGACTGCTTTGAGAAG
GCCAGCAAGGTCAAGCTGGCACCTGAGAGGATTGCCGATGGCACCATGGCATTTATGTTT
GAATCATCTTTAAGTCTGGCGGTCACAAAGTGGGGACTCAAGGCCTCCAGGTGTTTGGAT
GAGAACTACCACAAGTGCTGGGAGCCACTCAAGAGCCACTTCACTCCCAACTCCAGGAAC
CCAGCAGAACCTAATTGA
Enzyme 1 GenBank Gene ID U63008 Link Image
Enzyme 1 GeneCard ID HGD Link Image
Enzyme 1 GenAtlas ID HGD Link Image
Enzyme 1 HGNC ID HGNC:4892 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q13.33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Fernandez-Canon JM, Granadino B, Beltran-Valero de Bernabe D, Renedo M, Fernandez-Ruiz E, Penalva MA, Rodriguez de Cordoba S: The molecular basis of alkaptonuria. Nat Genet. 1996 Sep;14(1):19-24. [PubMed Link Image]
  2. Granadino B, Beltran-Valero de Bernabe D, Fernandez-Canon JM, Penalva MA, Rodriguez de Cordoba S: The human homogentisate 1,2-dioxygenase (HGO) gene. Genomics. 1997 Jul 15;43(2):115-22. [PubMed Link Image]
  3. Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE: Crystal structure of human homogentisate dioxygenase. Nat Struct Biol. 2000 Jul;7(7):542-6. [PubMed Link Image]
  4. Gehrig A, Schmidt SR, Muller CR, Srsen S, Srsnova K, Kress W: Molecular defects in alkaptonuria. Cytogenet Cell Genet. 1997;76(1-2):14-6. [PubMed Link Image]
  5. Beltran-Valero de Bernabe D, Granadino B, Chiarelli I, Porfirio B, Mayatepek E, Aquaron R, Moore MM, Festen JJ, Sanmarti R, Penalva MA, de Cordoba SR: Mutation and polymorphism analysis of the human homogentisate 1, 2-dioxygenase gene in alkaptonuria patients. Am J Hum Genet. 1998 Apr;62(4):776-84. [PubMed Link Image]
  6. Higashino K, Liu W, Ohkawa T, Yamamoto T, Fukui K, Ohno M, Imanishi H, Iwasaki A, Amuro Y, Hada T: A novel point mutation associated with alkaptonuria. Clin Genet. 1998 Mar;53(3):228-9. [PubMed Link Image]
  7. Beltran-Valero de Bernabe D, Jimenez FJ, Aquaron R, Rodriguez de Cordoba S: Analysis of alkaptonuria (AKU) mutations and polymorphisms reveals that the CCC sequence motif is a mutational hot spot in the homogentisate 1,2 dioxygenase gene (HGO). Am J Hum Genet. 1999 May;64(5):1316-22. [PubMed Link Image]
  8. Felbor U, Mutsch Y, Grehn F, Muller CR, Kress W: Ocular ochronosis in alkaptonuria patients carrying mutations in the homogentisate 1,2-dioxygenase gene. Br J Ophthalmol. 1999 Jun;83(6):680-3. [PubMed Link Image]
  9. Muller CR, Fregin A, Srsen S, Srsnova K, Halliger-Keller B, Felbor U, Seemanova E, Kress W: Allelic heterogeneity of alkaptonuria in Central Europe. Eur J Hum Genet. 1999 Sep;7(6):645-51. [PubMed Link Image]
  10. Beltran-Valero de Bernabe D, Peterson P, Luopajarvi K, Matintalo P, Alho A, Konttinen Y, Krohn K, Rodriguez de Cordoba S, Ranki A: Mutational analysis of the HGO gene in Finnish alkaptonuria patients. J Med Genet. 1999 Dec;36(12):922-3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13120
Enzyme 2 Name Uncharacterized protein GSTZ1
Enzyme 2 Synonyms
  1. Glutathione transferase zeta 1
  2. Maleylacetoacetate isomerase, isoform CRA_a
Enzyme 2 Gene Name GSTZ1
Enzyme 2 Protein Sequence >Uncharacterized protein GSTZ1 
MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
Enzyme 2 Number of Residues 161
Enzyme 2 Molecular Weight 17896
Enzyme 2 Theoretical pI 5.76
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID A6NNB8 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A6NNB8_HUMAN Link Image
Enzyme 2 PDB ID 1FW1 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 AC007954 Link Image
Enzyme 2 GeneCard ID A6NNB8 Link Image
Enzyme 2 GenAtlas ID GSTZ1 Link Image
Enzyme 2 HGNC ID HGNC:4643 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available