1.13.11.72: 2-hydroxyethylphosphonate dioxygenase
This is an abbreviated version!
For detailed information about 2-hydroxyethylphosphonate dioxygenase, go to the full flat file.
Reaction
Synonyms
HEPD, hydroxyethylphosphonate dioxygenase, PhdP, phpD
ECTree
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General Information
General Information on EC 1.13.11.72 - 2-hydroxyethylphosphonate dioxygenase
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evolution
physiological function
additional information
2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS) are non-heme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Both HEPD and MPnS generate a methylphosphonate radical. Substrate labeling experiments lead to a mechanistic hypothesis in which the fate of a common intermediate determines product identity, overview. Primary sequences and homology modeling suggest that the architectures of the active sites of HEPD and MPnS are similar
evolution
one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle
evolution
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2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS) are non-heme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Both HEPD and MPnS generate a methylphosphonate radical. Substrate labeling experiments lead to a mechanistic hypothesis in which the fate of a common intermediate determines product identity, overview. Primary sequences and homology modeling suggest that the architectures of the active sites of HEPD and MPnS are similar
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evolution
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one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle
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2-hydroxyethylphosphonate dioxygenase (HEPD) cleaves the C1-C2 bond of its substrate to afford hydroxymethylphosphonate on the biosynthetic pathway to the commercial herbicide phosphinothricin
physiological function
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2-hydroxyethylphosphonate dioxygenase (HEPD) cleaves the C1-C2 bond of its substrate to afford hydroxymethylphosphonate on the biosynthetic pathway to the commercial herbicide phosphinothricin
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the active site metal is coordinated by 2-His-1-Glu on one face of a pseudooctrahedron
additional information
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the active site metal is coordinated by 2-His-1-Glu on one face of a pseudooctrahedron
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