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
1.13.11.72 2-hydroxyethylphosphonate dioxygenaseAdvanced search results
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Engineering on EC 1.13.11.72 - 2-hydroxyethylphosphonate dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E176A
site-directed mutagenesis, the mutant enzyme shows similar activity as the wild-type enzyme. Like the wild-type enzyme, the mutant HEPD-E176A produces hydroxymethylphosphonate and formate as its only detectable products upon incubation with Fe(II), hydroxyethylphosphonate, and O2
E176H
R90A
large decrease in ratio kcat/Km, mutant cannot be saturated in O2
Y98F
large decrease in ratio kcat/Km, mutant cannot be saturated in O2. Mutant produces methylphosphonate as a minor side product
E176A
-
site-directed mutagenesis, the mutant enzyme shows similar activity as the wild-type enzyme. Like the wild-type enzyme, the mutant HEPD-E176A produces hydroxymethylphosphonate and formate as its only detectable products upon incubation with Fe(II), hydroxyethylphosphonate, and O2
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E176H
E176H
site-directed mutagenesis, the mutant is bifunctional exhibiting the activity of both 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73). The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaces. More HEPD activity is observed when the reaction is carried out with (R)-2-[2-2H1]-hydroxyethylphosphonate
E176H
the mutant catalyzes the transformation of 2-hydroxypropylphosphonate to methylphosphonate
E176H
-
site-directed mutagenesis, the mutant is bifunctional exhibiting the activity of both 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73). The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaces. More HEPD activity is observed when the reaction is carried out with (R)-2-[2-2H1]-hydroxyethylphosphonate
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E176H
-
the mutant catalyzes the transformation of 2-hydroxypropylphosphonate to methylphosphonate
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