1.13.11.73: methylphosphonate synthase
This is an abbreviated version!
For detailed information about methylphosphonate synthase, go to the full flat file.
Word Map on EC 1.13.11.73
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1.13.11.73
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dioxygenase
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oxygenases
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nonheme
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h-abstraction
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methane
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ocean
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deprotonate
- 1.13.11.73
- dioxygenase
- oxygenases
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nonheme
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h-abstraction
- methane
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ocean
-
deprotonate
Reaction
Synonyms
methylphosphonate synthase, mpnS
ECTree
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General Information
General Information on EC 1.13.11.73 - methylphosphonate synthase
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evolution
additional information
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apo MPnS homology modeling using the crystal structure of Cd2+-substituted HEPD, EC 1.13.11.72, in complex with substrate 2-hydroxyethylphosphonate, PDB ID 3GBF
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2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) 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
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one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) and methylphosphonate synthase (MPnS) 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