We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
IUBMB Comments 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 .
Synonyms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MetaCyc
dehydrophos biosynthesis, fosfomycin biosynthesis, methylphosphonate biosynthesis, phosalacine biosynthesis, phosphinothricin tripeptide biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxyethylphosphonate + NAD+
phosphonoacetaldehyde + NADH + H+
-
Substrates: 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
r
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
phosphonoacetaldehyde + NADPH + H+
2-hydroxyethylphosphonate + NADP+
-
Substrates: 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
?
additional information
?
-
-
Substrates: no reaction is observed with hydroxymethylphosphonate and 3-hydroxypropylphosphonate
?
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
-
Substrates: the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
?
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
-
Substrates: 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
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphonoacetaldehyde + NADH + H+
2-hydroxyethylphosphonate + NAD+
-
Substrates: the enzyme catalyzes a step in the phosphinothricin tripeptide pathway
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
NADH
-
PhpC is an NADH-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
the iron content of PhpC is less than 5%
Zn2+
-
Zn2+ is required for enzymatic activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EDTA
-
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0193
NADH
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
0.185
phosphonoacetaldehyde
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.41
phosphonoacetaldehyde
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.2
phosphonoacetaldehyde
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7
-
phosphonoacetaldehyde reduction is more favorable under neutral conditions (optimal pH at 7.0)
9
-
2-hydroxyethylphosphonate oxidation is favored under basic conditions (optimal pH at 9.0)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
DSM 40736
-
-
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PHPC_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
395
0
40987
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
html completed
show
top
