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show all sequences of 1.1.1.309

Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways

Shao, Z.; Blodgett, J.A.V.; Circello, B.T.; Eliot, A.C.; Woodyer, R.; Li, G.; van der Donk, W.A.; Metcalf, W.W.; Zhao, H.; J. Biol. Chem. 283, 23161-23168 (2008)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
approximately 0.02-0.025 mM PhpC is incubated with 20-25 mM EDTA at 4C until the activity is completely abolished (usually 1-2 h)
Streptomyces viridochromogenes
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0193
-
NADH
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
0.185
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
the iron content of PhpC is less than 5%
Streptomyces viridochromogenes
Zn2+
Zn2+ is required for enzymatic activity
Streptomyces viridochromogenes
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces viridochromogenes
-
-
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces viridochromogenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxyethylphosphonate + NAD+
the catalytic efficiency of phosphonoacetaldehyde reduction is 377fold greater than that of the reverse reaction, and even at pH 9.0, the catalytic efficiency of the forward reaction is still 11fold greater than that of the reverse reaction
712363
Streptomyces viridochromogenes
phosphonoacetaldehyde + NADH + H+
-
-
-
r
additional information
no reaction is observed with hydroxymethylphosphonate and 3-hydroxypropylphosphonate
712363
Streptomyces viridochromogenes
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
gel filtration
Streptomyces viridochromogenes
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.41
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
phosphonoacetaldehyde reduction is more favorable under neutral conditions (optimal pH at 7.0)
Streptomyces viridochromogenes
9
-
2-hydroxyethylphosphonate oxidation is favored under basic conditions (optimal pH at 9.0)
Streptomyces viridochromogenes
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
PhpC is an NADH-dependent enzyme
Streptomyces viridochromogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
PhpC is an NADH-dependent enzyme
Streptomyces viridochromogenes
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
approximately 0.02-0.025 mM PhpC is incubated with 20-25 mM EDTA at 4C until the activity is completely abolished (usually 1-2 h)
Streptomyces viridochromogenes
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0193
-
NADH
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
0.185
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
the iron content of PhpC is less than 5%
Streptomyces viridochromogenes
Zn2+
Zn2+ is required for enzymatic activity
Streptomyces viridochromogenes
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
2-hydroxyethylphosphonate + NAD+
the catalytic efficiency of phosphonoacetaldehyde reduction is 377fold greater than that of the reverse reaction, and even at pH 9.0, the catalytic efficiency of the forward reaction is still 11fold greater than that of the reverse reaction
712363
Streptomyces viridochromogenes
phosphonoacetaldehyde + NADH + H+
-
-
-
r
additional information
no reaction is observed with hydroxymethylphosphonate and 3-hydroxypropylphosphonate
712363
Streptomyces viridochromogenes
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
gel filtration
Streptomyces viridochromogenes
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.41
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
phosphonoacetaldehyde reduction is more favorable under neutral conditions (optimal pH at 7.0)
Streptomyces viridochromogenes
9
-
2-hydroxyethylphosphonate oxidation is favored under basic conditions (optimal pH at 9.0)
Streptomyces viridochromogenes
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.2
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Streptomyces viridochromogenes
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.2
-
phosphonoacetaldehyde
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
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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