Information on EC 1.1.1.309 - phosphonoacetaldehyde reductase (NADH)

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The expected taxonomic range for this enzyme is: Streptomyces viridochromogenes

EC NUMBER
COMMENTARY hide
1.1.1.309
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RECOMMENDED NAME
GeneOntology No.
phosphonoacetaldehyde reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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dehydrophos biosynthesis
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fosfomycin biosynthesis
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phosalacine biosynthesis
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phosphinothricin tripeptide biosynthesis
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxyethylphosphonate:NAD+ oxidoreductase
The enzyme from Streptomyces viridochromogenes catalyses a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate. The preferred cofactor is NADH, lower activity with NADPH [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxyethylphosphonate + NAD+
phosphonoacetaldehyde + NADH + H+
show the reaction diagram
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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
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r
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
show the reaction diagram
phosphonoacetaldehyde + NADPH + H+
2-hydroxyethylphosphonate + NADP+
show the reaction diagram
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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
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?
additional information
?
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no reaction is observed with hydroxymethylphosphonate and 3-hydroxypropylphosphonate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
show the reaction diagram
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the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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the iron content of PhpC is less than 5%
Zn2+
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Zn2+ is required for enzymatic activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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approximately 0.02-0.025 mM PhpC is incubated with 20-25 mM EDTA at 4°C until the activity is completely abolished (usually 1-2 h)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0193
NADH
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
0.185
phosphonoacetaldehyde
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
phosphonoacetaldehyde
Streptomyces viridochromogenes
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
phosphonoacetaldehyde
Streptomyces viridochromogenes
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
1309
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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phosphonoacetaldehyde reduction is more favorable under neutral conditions (optimal pH at 7.0)
9
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2-hydroxyethylphosphonate oxidation is favored under basic conditions (optimal pH at 9.0)
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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gel filtration
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans
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