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Literature summary extracted from

  • Peck, S.C.; Chekan, J.R.; Ulrich, E.C.; Nair, S.K.; van der Donk, W.A.
    A common late-stage intermediate in catalysis by 2-hydroxyethyl-phosphonate dioxygenase and methylphosphonate synthase (2015), J. Am. Chem. Soc., 137, 3217-3220 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.72 recombinant expression of wild-type and mutant enzymes in Escherichia coli Streptomyces viridochromogenes
1.13.11.73 recombinant expression of the mutant enzyme in Escherichia coli Streptomyces viridochromogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.72 purified recombinant enzyme mutant E176H, X-ray diffraction structure determination and analysis at 1.75 A resolution Streptomyces viridochromogenes
1.13.11.73 purified recombinant enzyme mutant E176H, X-ray diffraction structure determination and analysis at 1.75 A resolution Streptomyces viridochromogenes

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.72 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 Streptomyces viridochromogenes
1.13.11.73 E176H site-directed mutagenesis, the HEPD, EC 1.13.11.72, mutant is bifunctional exhibiting the activity of both 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS). 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 Streptomyces viridochromogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.72 additional information
-
 additional information steady-state Michaelis-Menten kinetics of wild-type enzyme and mutant E176H Streptomyces viridochromogenes
1.13.11.73 additional information
-
 additional information steady-state Michaelis-Menten kinetics of mutant E176H Streptomyces viridochromogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.72 Fe2+ a non-heme iron oxygenase, Fe2+ is required for catalysis Streptomyces viridochromogenes
1.13.11.73 Fe2+ a non-heme iron oxygenase, Fe2+ is required for catalysis Streptomyces viridochromogenes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.72 2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes
-
 hydroxymethylphosphonate + formate
-
 ?
1.13.11.72 2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes DSM 40736
-
 hydroxymethylphosphonate + formate
-
 ?
1.13.11.73 2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes
-
 methylphosphonate + HCO3-
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.72 Streptomyces viridochromogenes Q5IW40
-
-
1.13.11.72 Streptomyces viridochromogenes DSM 40736 Q5IW40
-
-
1.13.11.73 Streptomyces viridochromogenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.72 recombinant wild-type and mutant enzymes from Escherichia coli Streptomyces viridochromogenes
1.13.11.73 recombinant mutant enzyme from Escherichia coli Streptomyces viridochromogenes

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.72 2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate catalytic mechanism Streptomyces viridochromogenes
a
1.13.11.73 2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3- catalytic mechanism Streptomyces viridochromogenes
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.72 2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
1.13.11.72 2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ?
1.13.11.73 2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes methylphosphonate + HCO3-
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.72 HEPD
-
 Streptomyces viridochromogenes
1.13.11.73 methylphosphonate synthase
-
 Streptomyces viridochromogenes
1.13.11.73 mpnS
-
 Streptomyces viridochromogenes

General Information

EC Number General Information Comment Organism
1.13.11.72 evolution 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 Streptomyces viridochromogenes
1.13.11.73 evolution 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 Streptomyces viridochromogenes