BRENDA - Enzyme Database show
show all sequences of 1.13.11.72

An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis

Cicchillo, R.M.; Zhang, H.; Blodgett, J.A.; Whitteck, J.T.; Li, G.; Nair, S.K.; van der Donk, W.A.; Metcalf, W.W.; Nature 459, 871-874 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Streptomyces viridochromogenes
Crystallization (Commentary)
Crystallization
Organism
to 1.8 A resolution. The overall structure consists of imperfect tandem repeats of a bi-domain architecture. Each of the repeats is composed of an all-alpha-helical domain linked to a beta-barrel fold characteristic of the cupin superfamily. A Cd(II) ion is situated at the base of the active site and is coordinated by residues His 129, Glu 176 and His 182
Streptomyces viridochromogenes
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
mononuclear non-haem iron(II)-dependent enzyme
Streptomyces viridochromogenes
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces viridochromogenes
Q5IW40
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxyethylphosphonate + O2
-
720539
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
all four electrons required for reduction of O2 are provided by the substrate. Occurence of an intermediate species in which oxygen derived from O2 exchanges with water
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no cofactors required
Streptomyces viridochromogenes
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Streptomyces viridochromogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no cofactors required
Streptomyces viridochromogenes
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 1.8 A resolution. The overall structure consists of imperfect tandem repeats of a bi-domain architecture. Each of the repeats is composed of an all-alpha-helical domain linked to a beta-barrel fold characteristic of the cupin superfamily. A Cd(II) ion is situated at the base of the active site and is coordinated by residues His 129, Glu 176 and His 182
Streptomyces viridochromogenes
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
mononuclear non-haem iron(II)-dependent enzyme
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
-
720539
Streptomyces viridochromogenes
hydroxymethylphosphonate + formate
all four electrons required for reduction of O2 are provided by the substrate. Occurence of an intermediate species in which oxygen derived from O2 exchanges with water
-
-
?
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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1
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1
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4
1
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1
1
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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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2
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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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1
1
1
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4
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1
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1
1
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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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4
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6
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1
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6
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2
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2
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6
6
719655
Whitteck
On the stereochemistry of 2-hy ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
133
4236-4239
2011
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3
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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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1
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719645
Whitteck
Hydroperoxylation by hydroxyet ...
Streptomyces viridochromogenes
J. Am. Chem. Soc.
131
16225-16232
2009
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1
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1
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6
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720539
Cicchillo
An unusual carbon-carbon bond ...
Streptomyces viridochromogenes
Nature
459
871-874
2009
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1
1
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