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Literature summary for 1.13.11.73 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
Search for more literature for 1.13.11.73

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the mutant enzyme in Escherichia coli Streptomyces viridochromogenes

Crystallization (Commentary)

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

Protein Variants

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state Michaelis-Menten kinetics of mutant E176H Streptomyces viridochromogenes

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes
-
 methylphosphonate + HCO3-
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutant enzyme from Escherichia coli Streptomyces viridochromogenes

Reaction

Reaction Comment Organism Reaction ID
2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3- catalytic mechanism Streptomyces viridochromogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes methylphosphonate + HCO3-
-
 ?

Synonyms

Synonyms Comment Organism
methylphosphonate synthase
-
 Streptomyces viridochromogenes
mpnS
-
 Streptomyces viridochromogenes

General Information

General Information Comment Organism
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