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EC Tree
The expected taxonomic range for this enzyme is: Bacillus subtilis group
Synonyms
BacG, YwfH,
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BacG
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YwfH
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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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(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+
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+
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+
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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+
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+
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 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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?
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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
-
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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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
-
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
-
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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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
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
physiological function
the enzyme is involved in biosynthesis of bacilysin, a nonribosomally synthesized dipeptide antibiotic composed of L -alanine and L -anticapsin
physiological function
the enzyme is involved in the biosynthesis of the antibiotic bacilysin
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
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
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A7Z9Z0_BACVZ
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
259
0
27929
TrEMBL
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BACG_BACSU
Bacillus subtilis (strain 168)
259
0
28022
Swiss-Prot
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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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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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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
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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 (P39644), Bacillus subtilis 168 (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 (P39644), Bacillus subtilis 168 (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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1.3.1.B7 (3E)-3-[(4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate reductase [NAD(P)H]
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