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Literature summary for 1.13.11.72 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 1.13.11.72

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes 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 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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state Michaelis-Menten kinetics of wild-type enzyme and 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
-
 hydroxymethylphosphonate + formate
-
 ?
2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes DSM 40736
-
 hydroxymethylphosphonate + formate
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes Q5IW40
-
-
Streptomyces viridochromogenes DSM 40736 Q5IW40
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Streptomyces viridochromogenes

Reaction

Reaction Comment Organism Reaction ID
2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate catalytic mechanism Streptomyces viridochromogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ?

Synonyms

Synonyms Comment Organism
HEPD
-
 Streptomyces viridochromogenes

General Information

General Information Comment Organism
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