BRENDA - Enzyme Database show
show all sequences of 1.1.1.309

Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide

Blodgett, J.A.; Thomas, P.M.; Li, G.; Velasquez, J.E.; van der Donk, W.A.; Kelleher, N.L.; Metcalf, W.W.; Nat. Chem. Biol. 3, 480-485 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans
Streptomyces viridochromogenes
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphonoacetaldehyde + NADH + H+
Streptomyces viridochromogenes
the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
2-hydroxyethylphosphonate + NAD+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces viridochromogenes
-
DSM 40736
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces viridochromogenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphonoacetaldehyde + NADH + H+
the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NAD+
-
-
-
?
phosphonoacetaldehyde + NADH + H+
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NAD+
-
-
-
?
phosphonoacetaldehyde + NADPH + H+
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NADP+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Streptomyces viridochromogenes
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Streptomyces viridochromogenes
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
Streptomyces viridochromogenes
NADPH
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
Streptomyces viridochromogenes
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans
Streptomyces viridochromogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
Streptomyces viridochromogenes
NADPH
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
Streptomyces viridochromogenes
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphonoacetaldehyde + NADH + H+
Streptomyces viridochromogenes
the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
2-hydroxyethylphosphonate + NAD+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Streptomyces viridochromogenes
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphonoacetaldehyde + NADH + H+
the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NAD+
-
-
-
?
phosphonoacetaldehyde + NADH + H+
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NAD+
-
-
-
?
phosphonoacetaldehyde + NADPH + H+
the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor
705845
Streptomyces viridochromogenes
2-hydroxyethylphosphonate + NADP+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Streptomyces viridochromogenes
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Streptomyces viridochromogenes
General Information
General Information
Commentary
Organism
malfunction
the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide
Streptomyces viridochromogenes
General Information (protein specific)
General Information
Commentary
Organism
malfunction
the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide
Streptomyces viridochromogenes
Other publictions for EC 1.1.1.309
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)
712363
Shao
Biosynthesis of 2-hydroxyethyl ...
Streptomyces viridochromogenes
J. Biol. Chem.
283
23161-23168
2008
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705845
Blodgett
Unusual transformations in the ...
Streptomyces viridochromogenes
Nat. Chem. Biol.
3
480-485
2007
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