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Enzyme Nomenclature
Information on EC 1.3.1.B7 - (3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate reductase [NAD(P)H]
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The expected taxonomic range for this enzyme is: Bacillus subtilis group
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EC NUMBER 
COMMENTARY 
1.3.1.B7
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate reductase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD(P)+ = 3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD(P)H + H+
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-
-
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SYSTEMATIC NAME
IUBMB Comments
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate:NA(P)D+ oxidoreductase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
transcription of the bac operon and of the ywfH gene in Bacillus amyloliquefaciens FZB42 is positively controlled by the DegU global regulator protein
metabolism
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transcription of the bac operon and of the ywfH gene in Bacillus amyloliquefaciens FZB42 is positively controlled by the DegU global regulator protein
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physiological function
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the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
physiological function
-
the enzyme is involved in the biosynthesis of the antibiotic bacilysin
physiological function
the enzyme is involved in biosynthesis of bacilysin, a nonribosomally synthesized dipeptide antibiotic composed of L -alanine and L -anticapsin
physiological function
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the enzyme is involved in biosynthesis of bacilysin, a nonribosomally synthesized dipeptide antibiotic composed of L -alanine and L -anticapsin
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physiological function
-
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin; the enzyme is involved in the biosynthesis of the antibiotic bacilysin
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADPH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADP+
-
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
the enzyme is involved in the biosynthesis of the antibiotic bacilysin
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
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the enzyme is involved in the biosynthesis of the antibiotic bacilysin
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
P39644
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
P39644
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
-
-
?
(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NADH + H+
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate + NAD+
-
-
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.178
NADPH
-
pH and temperature not specified in the publication, wild-type enzyme
0.365
NADPH
-
pH and temperature not specified in the publication, mutant enzyme K113A
323
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S250A
345
NADPH
-
pH and temperature not specified in the publication, mutant enzyme N158A
528
NADPH
-
pH and temperature not specified in the publication, mutant enzyme Y117A
614
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S155A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0344
NADPH
-
pH and temperature not specified in the publication, wild-type enzyme
0.143
NADPH
-
pH and temperature not specified in the publication, mutant enzyme N158A
0.146
NADPH
-
pH and temperature not specified in the publication, mutant enzyme K113A
0.175
NADPH
-
pH and temperature not specified in the publication, mutant enzyme Y117A
0.216
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S155A
0.286
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S250A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
NADPH
-
pH and temperature not specified in the publication, mutant enzyme Y117A
0.035
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S155A
0.04
NADPH
-
pH and temperature not specified in the publication, mutant enzyme K113A
0.042
NADPH
-
pH and temperature not specified in the publication, mutant enzyme N158A
0.089
NADPH
-
pH and temperature not specified in the publication, mutant enzyme S250A
0.193
NADPH
-
pH and temperature not specified in the publication, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of YwfH is determined in three conformational states. These represent apo YwfH, the YwfH/NADPH complex and an apo-like form
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.B7)
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