Homogentisate 1,2-dioxygenase

homogentisate 1,2-dioxygenase
3D rendering of Homogentisate Dioxygenase with active site amino acid residues and Iron atom colored. Histidine is the tan color, Glutamate the red color, and Iron is the blue.
Identifiers
EC no.1.13.11.5
CAS no.9029-49-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
homogentisate 1,2-dioxygenase (homogentisate oxidase)
Identifiers
SymbolHGD
Alt. symbolsAKU
NCBI gene3081
HGNC4892
OMIM607474
RefSeqXM_001125882
UniProtQ93099
Other data
EC number1.13.11.5
LocusChr. 3 q21-q23
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StructuresSwiss-model
DomainsInterPro

Homogentisate 1,2-dioxygenase (homogentisic acid oxidase, homogentisate oxidase, homogentisicase) is an 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 breakdown of the amino acids tyrosine and phenylalanine.[1] HGD appears in the metabolic pathway of tyrosine and phenylalanine degradation once the molecule homogentisate is produced. Homogentisate reacts with HGD to produce maleylacetoacetate, which then is further used in the metabolic pathway. HGD requires the use of Fe2+ and O2 in order to cleave the aromatic ring of homogentisate.[2]

  1. ^ Titus GP, Mueller HA, Burgner J, Rodríguez De Córdoba S, Peñalva MA, Timm DE (Jul 2000). "Crystal structure of human homogentisate dioxygenase". Nature Structural Biology. 7 (7): 542–6. doi:10.1038/76756. hdl:10261/71724. PMID 10876237. S2CID 6219553.
  2. ^ Borowski T, Georgiev V, Siegbahn PE (Dec 2005). "Catalytic reaction mechanism of homogentisate dioxygenase: a hybrid DFT study". Journal of the American Chemical Society. 127 (49): 17303–14. doi:10.1021/ja054433j. PMID 16332080.