D
IPR046451

Homogentisate 1,2-dioxygenase, C-terminal domain

InterPro entry
Short nameHgmA_C
Overlapping
homologous
superfamilies
 

Description

Alkaptonuria (AKU), a rare hereditary disorder, was the first disease to be interpreted as an inborn error of metabolism. The deficiency causes homogentisic aciduria, ochronosis, and arthritis. AKU patients are deficient for homogentisate 1,2 dioxygenase (HGD) (
1.13.11.5
), the enzyme that mediates the conversion of homogentisate to maleylacetoacetate, a step in the catabolism of both tyrosine and phenylalanine. The structure of this protein 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
[2, 1]
.

This group of proteins includes human HDG and homologues from eukaryotes, bacteria and some archaeal species.

This entry represents the C-terminal active site domain of HGD.

References

1.Crystal structure of human homogentisate dioxygenase. Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE. Nat. Struct. Biol. 7, 542-6, (2000). View articlePMID: 10876237

2.The molecular basis of alkaptonuria. Fernandez-Canon JM, Granadino B, Beltran-Valero de Bernabe D, Renedo M, Fernandez-Ruiz E, Penalva MA, Rodriguez de Cordoba S. Nat Genet 14, 19-24, (1996). PMID: 8782815

Cross References

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