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show all sequences of 1.13.11.72

O-H activation by an unexpected ferryl intermediate during catalysis by 2-hydroxyethylphosphonate dioxygenase

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.; J. Am. Chem. Soc. 139, 2045-2052 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli
Streptomyces viridochromogenes
Engineering
Amino acid exchange
Commentary
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
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow and multi-turnover steady-state kinetics
Streptomyces viridochromogenes
Metals/Ions
Metals/Ions
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes
-
hydroxymethylphosphonate + formate
-
-
?
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes DSM 40736
-
hydroxymethylphosphonate + formate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces viridochromogenes
Q5IW40
-
-
Streptomyces viridochromogenes DSM 40736
Q5IW40
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Streptomyces viridochromogenes
Reaction
Reaction
Commentary
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
Subunits
Commentary
Organism
?
x * 30000, recombinant enzyme, SDS-PAGE
Streptomyces viridochromogenes
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli
Streptomyces viridochromogenes
Engineering (protein specific)
Amino acid exchange
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow and multi-turnover steady-state kinetics
Streptomyces viridochromogenes
Metals/Ions (protein specific)
Metals/Ions
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes
-
hydroxymethylphosphonate + formate
-
-
?
2-hydroxyethylphosphonate + O2
Streptomyces viridochromogenes DSM 40736
-
hydroxymethylphosphonate + formate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Streptomyces viridochromogenes
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Subunits
Commentary
Organism
?
x * 30000, recombinant enzyme, SDS-PAGE
Streptomyces viridochromogenes
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.13.11.72
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745178
Peck
O-H activation by an unexpect ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
139
2045-2052
2017
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745390
Peck
Go it alone four-electron oxi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Biol. Inorg. Chem.
22
381-394
2017
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745162
Peck
A common late-stage intermedi ...
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
J. Am. Chem. Soc.
137
3217-3220
2015
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720308
Du
Water-dependent reaction pathw ...
Streptomyces viridochromogenes
J. Phys. Chem. B
116
11837-11844
2012
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718907
Peck
Mechanism and substrate recogn ...
Streptomyces viridochromogenes
Biochemistry
50
6598-6605
2011
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719655
Whitteck
On the stereochemistry of 2-hy ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
133
4236-4239
2011
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719648
Hirao
Ferric superoxide and ferric h ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
132
17901-17909
2010
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719645
Whitteck
Hydroperoxylation by hydroxyet ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
131
16225-16232
2009
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720539
Cicchillo
An unusual carbon-carbon bond ...
Streptomyces viridochromogenes
Nature
459
871-874
2009
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