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Information on EC 1.3.1.B7 - (3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate reductase [NAD(P)H] for references in articles please use BRENDA:EC1.3.1.B7Please 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: Bacillus subtilis group
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1.3.1.B7
preliminary BRENDA-supplied EC number
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(3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate reductase [NAD(P)H]
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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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3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate:NA(P)D+ oxidoreductase
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BacG
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YwfH
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UniProt
brenda
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UniProt
brenda
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SwissProt
brenda
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brenda
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SwissProt
brenda
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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
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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
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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; the enzyme is involved in the biosynthesis of the antibiotic bacilysin
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(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+
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(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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(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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(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
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?
(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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?
(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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(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+
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(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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?
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(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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(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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0.178
NADPH
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pH and temperature not specified in the publication, wild-type enzyme
0.365
NADPH
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pH and temperature not specified in the publication, mutant enzyme K113A
323
NADPH
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pH and temperature not specified in the publication, mutant enzyme S250A
345
NADPH
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pH and temperature not specified in the publication, mutant enzyme N158A
528
NADPH
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pH and temperature not specified in the publication, mutant enzyme Y117A
614
NADPH
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pH and temperature not specified in the publication, mutant enzyme S155A
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0.0344
NADPH
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pH and temperature not specified in the publication, wild-type enzyme
0.143
NADPH
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pH and temperature not specified in the publication, mutant enzyme N158A
0.146
NADPH
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pH and temperature not specified in the publication, mutant enzyme K113A
0.175
NADPH
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pH and temperature not specified in the publication, mutant enzyme Y117A
0.216
NADPH
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pH and temperature not specified in the publication, mutant enzyme S155A
0.286
NADPH
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pH and temperature not specified in the publication, mutant enzyme S250A
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0.033
NADPH
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pH and temperature not specified in the publication, mutant enzyme Y117A
0.035
NADPH
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pH and temperature not specified in the publication, mutant enzyme S155A
0.04
NADPH
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pH and temperature not specified in the publication, mutant enzyme K113A
0.042
NADPH
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pH and temperature not specified in the publication, mutant enzyme N158A
0.089
NADPH
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pH and temperature not specified in the publication, mutant enzyme S250A
0.193
NADPH
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pH and temperature not specified in the publication, wild-type enzyme
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61500
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analytical size-exclusion chromatography
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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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expression in Escherichia coli
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K113A
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kcat/Km is 4.9fold lower than the wild-type value
N158A
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kcat/Km is 4.6fold lower than the wild-type value
S155A
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kcat/Km is 5.5fold lower than the wild-type value
S250A
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kcat/Km is 2.2fold lower than the wild-type value
Y117A
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kcat/Km is 5.8fold lower than the wild-type value
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BACG_BACSU
Bacillus subtilis (strain 168)
259
28022
Swiss-Prot
A7Z9Z0_BACVZ
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
259
27929
TrEMBL
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Rajavel, M.; Perinbam, K.; Gopal, B.
Structural insights into the role of Bacillus subtilis YwfH (BacG) in tetrahydrotyrosine synthesis
Acta Crystallogr. Sect. D
69
324-332
2013
Bacillus subtilis
brenda
Mahlstedt, S.A.; Walsh, C.T.
Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis
Biochemistry
49
912-923
2010
Bacillus subtilis 168 (P39644), Bacillus subtilis (P39644)
brenda
Parker, J.B.; Walsh, C.T.
Stereochemical outcome at four stereogenic centers during conversion of prephenate to tetrahydrotyrosine by BacABGF in the bacilysin pathway
Biochemistry
51
5622-5632
2012
Bacillus subtilis 168 (P39644), Bacillus subtilis (P39644)
brenda
Mariappan, A.; Makarewicz, O.; Chen, X.H.; Borriss, R.
Two-component response regulator DegU controls the expression of bacilysin in plant-growth-promoting bacterium Bacillus amyloliquefaciens FZB42
J. Mol. Microbiol. Biotechnol.
22
114-125
2012
Bacillus amyloliquefaciens (A7Z9Z0), Bacillus amyloliquefaciens FZB42 (A7Z9Z0)
brenda
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