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Literature summary extracted from

  • Titus, G.P.; Mueller, H.A.; Burgner, J.; Rodriguez de Cordoba, S.; Penalva, M.A.; Timm, D.E.
    Crystal structure of human homogentisate dioxygenase (2000), Nat. Struct. Biol., 7, 542-546.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.13.11.5 medicine
-
 Mus musculus
1.13.11.5 medicine HGO deficiency causes alkaptonuria, inherited as a recessive Mendelian trait, HGO inhibitors may be useful in the treatment of hereditary tyrosinemia type I, HT1 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.5 crystal structures of apo-HGO and HGO containing an iron Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.5 additional information
-
 Mus musculus
1.13.11.5 additional information 20 missence mutations in HGO from alkaptonuria patients Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.5 Fe2+
-
 Mus musculus
1.13.11.5 Fe2+
-
 Bos taurus
1.13.11.5 Fe2+ contains a nonheme Fe2+ at the active site, that is coordinated near the interface between subunits in the HGO trimer by Glu-341, His-335 and His-371 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.5 150000
-
-
 Mus musculus
1.13.11.5 254000
-
-
 Bos taurus
1.13.11.5 424000 478000 equilibrium sedimentation studies Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.5 homogentisate + O2 Mus musculus
-
 4-maleylacetoacetate
-
 ?
1.13.11.5 homogentisate + O2 Homo sapiens enzyme cleaves the aromatic ring during the metabolic degradation of phenylalanine and tyrosine 4-maleylacetoacetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.5 Bos taurus
-
-
-
1.13.11.5 Homo sapiens
-
-
-
1.13.11.5 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.5
-
 Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.5 homogentisate + O2 = 4-maleylacetoacetate catalytic mechanism Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.5 homogentisate + O2
-
 Mus musculus 4-maleylacetoacetate
-
 ?
1.13.11.5 homogentisate + O2 utilizes a nonheme iron to incorporate both atoms of molecular oxygen into homogentisate, identical with 2,5-dihydroxyphenylacetate Homo sapiens 4-maleylacetoacetate
-
 ?
1.13.11.5 homogentisate + O2 enzyme cleaves the aromatic ring during the metabolic degradation of phenylalanine and tyrosine Homo sapiens 4-maleylacetoacetate
-
 ?
1.13.11.5 additional information enzyme structure, conformation of the active site, enzyme contains a 280-residue N-terminal domain and a 140-residue C-terminal domain, associated as a hexamer arranged as a dimer of trimers Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.5 hexamer hexamer arranged as a dimer of trimers, subunit structure, functional importance of the hexamer in vivo Homo sapiens