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Literature summary for 1.13.11.72 extracted from

  • Peck, S.C.; Wang, C.; Dassama, L.M.; Zhang, B.; Guo, Y.; Rajakovich, L.J.; Bollinger, J.M.; Krebs, C.; van der Donk, W.A.
    O-H activation by an unexpected ferryl intermediate during catalysis by 2-hydroxyethylphosphonate dioxygenase (2017), J. Am. Chem. Soc., 139, 2045-2052 .
    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

Protein Variants

Protein Variants Comment Organism
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 Streptomyces viridochromogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped-flow and multi-turnover steady-state kinetics Streptomyces viridochromogenes

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for catalysis, the mechanism involves activation of an O-H bond by the ferryl complex 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 the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, a mechanism that involves activation of an O-H bond by the ferryl complex is proposed. The isotope-sensitive C-H-cleavage step is not primarily rate-limiting for the overall catalytic cycle. The reaction does exhibit a significant 2H-kinetic isotope effect on kcat/Km for O2, which implies reversible formation of the C-H-cleaving intermediate 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 the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, the mechanism involves activation of an O-H bond by the ferryl complex. Maximal accumulation of the intermediate requires both the presence of deuterium in the substrate and, importantly, the use of 2H2O as solvent Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ?
2-hydroxyethylphosphonate + O2 the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, the mechanism involves activation of an O-H bond by the ferryl complex. Maximal accumulation of the intermediate requires both the presence of deuterium in the substrate and, importantly, the use of 2H2O as solvent Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ?

Subunits

Subunits Comment Organism
? x * 30000, recombinant enzyme, SDS-PAGE Streptomyces viridochromogenes

Synonyms

Synonyms Comment Organism
HEPD
-
 Streptomyces viridochromogenes

General Information

General Information Comment Organism
physiological function 2-hydroxyethylphosphonate dioxygenase (HEPD) cleaves the C1-C2 bond of its substrate to afford hydroxymethylphosphonate on the biosynthetic pathway to the commercial herbicide phosphinothricin Streptomyces viridochromogenes