Data extracted from this reference:
Cloned(Commentary)
recombinant expression of wild-type and mutant enzymes in Escherichia coli
Streptomyces viridochromogenes
Engineering
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]
additional information
additional information
stopped-flow and multi-turnover steady-state kinetics
Streptomyces viridochromogenes
Metals/Ions
Fe2+
required for catalysis, the mechanism involves activation of an O-H bond by the ferryl complex
Streptomyces viridochromogenes
Natural Substrates/ Products (Substrates)
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
?
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes DSM 40736
hydroxymethylphosphonate + formate
?
Organism
Streptomyces viridochromogenes
Q5IW40
Streptomyces viridochromogenes DSM 40736
Q5IW40
Purification (Commentary)
recombinant wild-type and mutant enzymes from Escherichia coli
Streptomyces viridochromogenes
Reaction
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
Substrates and Products (Substrate)
2-hydroxyethylphosphonate + O2
745178
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
745178
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
?
2-hydroxyethylphosphonate + O2
745178
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
745178
Streptomyces viridochromogenes DSM 40736
hydroxymethylphosphonate + formate
?
Subunits
?
x * 30000, recombinant enzyme, SDS-PAGE
Streptomyces viridochromogenes
Synonyms
HEPD
Streptomyces viridochromogenes
Cloned(Commentary) (protein specific)
recombinant expression of wild-type and mutant enzymes in Escherichia coli
Streptomyces viridochromogenes
Engineering (protein specific)
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] (protein specific)
additional information
additional information
stopped-flow and multi-turnover steady-state kinetics
Streptomyces viridochromogenes
Metals/Ions (protein specific)
Fe2+
required for catalysis, the mechanism involves activation of an O-H bond by the ferryl complex
Streptomyces viridochromogenes
Natural Substrates/ Products (Substrates) (protein specific)
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
?
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes DSM 40736
hydroxymethylphosphonate + formate
?
Purification (Commentary) (protein specific)
recombinant wild-type and mutant enzymes from Escherichia coli
Streptomyces viridochromogenes
Substrates and Products (Substrate) (protein specific)
2-hydroxyethylphosphonate + O2
745178
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
745178
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
?
2-hydroxyethylphosphonate + O2
745178
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
745178
Streptomyces viridochromogenes DSM 40736
hydroxymethylphosphonate + formate
?
Subunits (protein specific)
?
x * 30000, recombinant enzyme, SDS-PAGE
Streptomyces viridochromogenes
General Information
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
General Information (protein specific)
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
Other publictions for EC 1.13.11.72
745178
Peck
O-H activation by an unexpect ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
139
2045-2052
2017
-
-
1
-
1
-
-
1
-
1
-
2
-
4
-
-
1
1
-
-
-
-
4
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
745390
Peck
Go it alone four-electron oxi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Biol. Inorg. Chem.
22
381-394
2017
-
-
-
1
-
-
-
-
-
1
-
2
-
4
-
-
-
1
-
-
-
-
6
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
745162
Peck
A common late-stage intermedi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
137
3217-3220
2015
-
-
1
1
1
-
-
1
-
1
-
2
-
4
-
-
1
1
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
720308
Du
Water-dependent reaction pathw ...
Streptomyces viridochromogenes
J. Phys. Chem. B
116
11837-11844
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
718907
Peck
Mechanism and substrate recogn ...
Streptomyces viridochromogenes
Biochemistry
50
6598-6605
2011
-
-
-
-
4
-
-
6
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
6
6
719655
Whitteck
On the stereochemistry of 2-hy ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
133
4236-4239
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719648
Hirao
Ferric superoxide and ferric h ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
132
17901-17909
2010
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719645
Whitteck
Hydroperoxylation by hydroxyet ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
131
16225-16232
2009
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
720539
Cicchillo
An unusual carbon-carbon bond ...
Streptomyces viridochromogenes
Nature
459
871-874
2009
-
-
1
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-