1.13.11.5: homogentisate 1,2-dioxygenase
This is an abbreviated version!
For detailed information about homogentisate 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.5
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1.13.11.5
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alkaptonuria
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ochronosis
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urine
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joint
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cartilage
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arthropathy
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sclera
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nitisinone
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arthroplasty
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discoloration
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darken
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maleylacetoacetate
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melanin-like
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calculi
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pyomelanin
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ultra-rare
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4-hydroxyphenylpyruvate
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slovakia
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medicine
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ntbc
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diagnostics
- 1.13.11.5
- alkaptonuria
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ochronosis
- urine
- joint
- cartilage
- arthropathy
- sclera
- nitisinone
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arthroplasty
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discoloration
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darken
- maleylacetoacetate
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melanin-like
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calculi
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pyomelanin
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ultra-rare
- 4-hydroxyphenylpyruvate
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slovakia
- medicine
- ntbc
- diagnostics
Reaction
Synonyms
EC 1.13.1.5, EC 1.99.2.5, ElHDO, HgD, HGDO, HGO, HGOa, HGOb, HmgA, homogentisate 1,2 dioxigenase, homogentisate 1,2 dioxygenase, homogentisate 1,2-dioxygenase, homogentisate dioxygenase, homogentisate oxidase, homogentisate oxygenase, homogentisate phytyl-transferase, homogentisic acid 1,2-dioxygenase, homogentisic acid oxidase, homogentisic acid oxygenase, homogentisic oxygenase, homogentisicase, HPT, HTO
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General Information
General Information on EC 1.13.11.5 - homogentisate 1,2-dioxygenase
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evolution
malfunction
physiological function
additional information
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the G161R natural mutation in the HGD gene occurs in a Hungarian population, originating from Slovakia, resists over 300 years, alkaptonuria phenotype overview
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
evolution
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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
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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
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
malfunction
enzyme mutations in the homogentisate 1,2 dioxygenase gene are responsible for alkaptonuria in patients among Jordanian population, genotyping, overview
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
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
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
malfunction
alkaptonuria is an inherited disease caused by homogentisate 1,2-dioxygenase deficiency
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
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
malfunction
ADH05034.1
disruption of the hmgA gene encoding homogentisate dioxygenase in BMB171 induces the accumulation of the homogentisic acid and provokes an increased pigment (pyomelanin) formation
malfunction
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disruption of the hmgA gene encoding homogentisate dioxygenase in BMB171 induces the accumulation of the homogentisic acid and provokes an increased pigment (pyomelanin) formation
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Vitis vinifera x Vitis vinifera
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involved in aromatic amino acid metabolism
physiological function
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involved in aromatic amino acid metabolism
physiological function
homogentisate 1,2-dioxygenase uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate, i.e 2,5-dihydroxyphenylacetate
physiological function
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homogentisate 1,2-dioxygenase is a potentially critical enzyme for regulation of pigment production
physiological function
essential enzyme for the catabolism of phenylalanine and tyrosine
physiological function
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homogentisate 1,2-dioxygenase is a potentially critical enzyme for regulation of pigment production
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physiological function
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homogentisate 1,2-dioxygenase uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate, i.e 2,5-dihydroxyphenylacetate
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HGD-BstXI genotypes show significant effects on cooking loss, drip loss, net meat weight, carcass weight, and eye muscle area. Also the HGD-HaeIII genotypes significantly affect cooking loss, muscle fibre diameter, shear force, drip loss, and carcass yield ratio. Phenotypes, overview
additional information
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mutations in homogentisate 1,2-dioxygenase cause alkaptonuria and subsequent ochronosis, an uncommon cause of backache. The phenotype includes limited spine mobility and chronic disk degeneration, overview
additional information
the active site pocket with its Fe2+ ion is freely accessible from the outside through a wide opening. Homogentisate binds as a monodentate ligand to Fe2+, and its interaction with Tyr346 invokes the folding of a loop over the active site, effectively shielding it from solvent. Binding of homogentisate is driven by enthalpy and is entropically disfavored as shown by anoxic isothermal titration calorimetry. Three different reaction cycle intermediates, i.e. superoxo:semiquinone-, alkylperoxo-, and product-bound intermediates. central role of Y346 in substrate binding and turnover
additional information
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the active site pocket with its Fe2+ ion is freely accessible from the outside through a wide opening. Homogentisate binds as a monodentate ligand to Fe2+, and its interaction with Tyr346 invokes the folding of a loop over the active site, effectively shielding it from solvent. Binding of homogentisate is driven by enthalpy and is entropically disfavored as shown by anoxic isothermal titration calorimetry. Three different reaction cycle intermediates, i.e. superoxo:semiquinone-, alkylperoxo-, and product-bound intermediates. central role of Y346 in substrate binding and turnover
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additional information
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HGD-BstXI genotypes show significant effects on cooking loss, drip loss, net meat weight, carcass weight, and eye muscle area. Also the HGD-HaeIII genotypes significantly affect cooking loss, muscle fibre diameter, shear force, drip loss, and carcass yield ratio. Phenotypes, overview
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