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Information on EC 1.1.1.309 - phosphonoacetaldehyde reductase (NADH) Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Streptomyces viridochromogenes
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phosphonoacetaldehyde reductase (NADH)
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2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+
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Phosphonate and phosphinate metabolism
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Biosynthesis of antibiotics
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fosfomycin biosynthesis
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phosalacine biosynthesis
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dehydrophos biosynthesis
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phosphinothricin tripeptide biosynthesis
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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].
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brenda
DSM 40736
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brenda
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malfunction
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the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide
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2-hydroxyethylphosphonate + NAD+
phosphonoacetaldehyde + NADH + H+
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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+
phosphonoacetaldehyde + NADPH + H+
2-hydroxyethylphosphonate + NADP+
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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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phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
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the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
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phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
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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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phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
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the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
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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
NADH
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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
NADH
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PhpC is an NADH-dependent enzyme
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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
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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)
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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
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0.41
phosphonoacetaldehyde
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
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2.2
phosphonoacetaldehyde
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in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
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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)
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overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans
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PHPC_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
395
40987
Swiss-Prot
A0A1V5MRJ4_9BACT
222
24082
TrEMBL
A0A1Q2Z931_9ACTN
389
41148
TrEMBL
A0A1V6IEF7_9BACT
138
15691
TrEMBL
A0A0U5HX34_9PROT
399
41744
TrEMBL
A0A0F2C607_9MICO
396
42406
TrEMBL
A0A142X244_9PLAN
420
44172
TrEMBL
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Blodgett, J.A.; Thomas, P.M.; Li, G.; Velasquez, J.E.; van der Donk, W.A.; Kelleher, N.L.; Metcalf, W.W.
Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide
Nat. Chem. Biol.
3
480-485
2007
Streptomyces viridochromogenes
brenda
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.
Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways
J. Biol. Chem.
283
23161-23168
2008
Streptomyces viridochromogenes
brenda
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