EC Number   |
General Information |
Reference |
|---|
    1.13.11.5 | evolution |
despite different folds, active site architectures, and Fe2+ coordination, extradiol dioxygenases can proceed through the same principal reaction intermediatesto catalyze the O2-dependent cleavage of aromatic rings. Convergent evolution of nonhomologous enzymes using the 2-His-1-carboxylate facial triad motif developed different solutions to stabilize closely related intermediates in unlike environments |
-, 726390 |
| 1.13.11.5 | evolution |
the G161R natural mutation in the HGD gene occurs in a Hungarian population, originating from Slovakia, resists over 300 years, alkaptonuria phenotype overview |
712909 |
| 1.13.11.5 | malfunction |
Alkaptonuria (AKU) is an ultra-rare disease caused by mutations in homogentisate 1,2-dioxygenase (HGD) enzyme, characterized by the loss of enzymatic activity and the accumulation of its substrate, homogentisic acid (HGA) in different tissues, leading to ochronosis and organ degeneration |
764530 |
| 1.13.11.5 | malfunction |
alkaptonuria is a rare autosomal recessive disease, associated with deficiency of homogentisate 1,2-dioxygenase activity in the liver. This leads to an accumulation of homogentisic acid and its oxidized derivatives in polymerized form in connective tissues, especially in joints. Homogentisic acid induces apoptosis in chondrocytes. N-acetylcysteine decreases apoptosis induced in chondrocytes by HGA, increases chondrocyte growth reduced by homogentisate, and partially restores proteoglycan release inhibited by homogentisate, the effect is improved by addition of ascorbic acid. Evaluation of antioxidant drugs for the treatment of ochronotic alkaptonuria, caused by homogentisate 1,2-dioxygenase activity mutation, in an in vitro human cell model, overview |
712561 |
| 1.13.11.5 | malfunction |
alkaptonuria is an autosomal recessive disorder, which is caused by a site-specific mutation(s) and thus, impairs the function of homogentisate-1, 2-dioxygenase |
765103 |
| 1.13.11.5 | malfunction |
alkaptonuria is an autosomal recessive disorder, which is caused by a site-specific mutations and thus, impairs the function of homogentisate-1,2-dioxygenase |
765103 |
| 1.13.11.5 | malfunction |
alkaptonuria is an inherited disease caused by homogentisate 1,2-dioxygenase deficiency |
764820 |
| 1.13.11.5 | malfunction |
alkaptonuria is an inherited disease that is caused by homogenticate accumulation. Deficiency or mutation in homogentisate 1,2-dioxygenase gene (chromosome 3q21-q23) lead to production of incorrectly folded or truncated enzyme |
764249 |
| 1.13.11.5 | malfunction |
alkaptonuria is caused by homogentisate 1,2-dioxygenase deficiency. Homogentisate 1,2-dioxygenase deficiency in the liver is responsible for homogentisic acid derived ochronotic pigmentation |
765293 |
| 1.13.11.5 | malfunction |
alkaptonuria results from defective homogentisate1,2-dioxygenase, causing degenerative arthropathy. The deposition of ochronotic pigment in joints is so far attributed to homogentisic acid produced by the liver, circulating in the blood and accumulating locally. Alkaptonuria osteoarticular cells produce the ochronotic pigment in loco and this may strongly contribute to induction of ochronotic arthropath |
725601 |
