Protein Family Models

Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers [1]. This entry represents the N-terminal domain which forms a jelly roll of beta-strands [1]. [1]. 10876237. Crystal structure of human homogentisate dioxygenase. Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE;. Nat Struct Biol 2000;7:542-546. (from Pfam)

Date:

2024-10-16

Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers [1]. This entry represents the C-terminal active site domain. [1]. 10876237. Crystal structure of human homogentisate dioxygenase. Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE;. Nat Struct Biol 2000;7:542-546. (from Pfam)

Date:

2024-10-16

homogentisate 1,2-dioxygenase catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate; belongs to the cupin superfamily

Date:

2024-09-24

Homogentisate 1,2-dioxygenase is an oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine. It is the enzyme missing in human disease alkaptonuria.

Gene:

hmgA

Date:

2021-04-27