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
-
ochronosis
- urine
- joint
- cartilage
- arthropathy
- sclera
- nitisinone
-
arthroplasty
-
discoloration
-
darken
- maleylacetoacetate
-
melanin-like
-
calculi
-
pyomelanin
-
ultra-rare
- 4-hydroxyphenylpyruvate
-
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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Metals Ions
Metals Ions on EC 1.13.11.5 - homogentisate 1,2-dioxygenase
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Fe2+
additional information
Fe2+
70% reduction of enzyme activity in crude extract in absence of Fe2+ and absolutely requirement for Fe2+ of the fusion protein of homogentisate dioxygenase and glutathione S-transferase, expressed in Escherichia coli
Fe2+
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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
Fe2+
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Fe2+ is an absolutely obligate cofactor and cannot be replaced by other divalent cations, highest enzyme activity in vitro at 2 mM Fe2+
Fe2+
required, ferrous ion content of 0.56 mol of iron per mol of protein, all twelve subunits in the a.u. contain fully occupied Fe sites, octahedral coordination for Fe2+ with two histidine residues (His331 and His367), the enzyme uses a mononuclear nonheme Fe2+ to catalyze the oxidative ring cleavage in the degradation of Tyr and Phe by producing maleylacetoacetate from homogentisate
Fe2+
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contains non-porphyrin iron, valence change of enzymic iron during reaction: ferric and ferrous iron
additional information
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other metallic ions, such as Fe3+, Co2+, Mn2+, Cu+ and Cu2+, cannot replace Fe2+