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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] and Organism(s) Bacillus subtilis and UniProt Accession P39644

for references in articles please use BRENDA:EC1.3.1.B7
preliminary BRENDA-supplied EC number
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Bacillus subtilis
UNIPROT: P39644 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacillus subtilis group
Synonyms
BacG, YwfH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
3-[(1R,4S)-4-hydroxycyclohex-2-en-1-yl]-2-oxopropanoate:NA(P)D+ oxidoreductase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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+
show the reaction diagram
(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+
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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+
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.178 - 614
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0344 - 0.286
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.193
NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
2 * 31000
61500
-
analytical size-exclusion chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 31000
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K113A
-
kcat/Km is 4.9fold lower than the wild-type value
N158A
-
kcat/Km is 4.6fold lower than the wild-type value
S155A
-
kcat/Km is 5.5fold lower than the wild-type value
S250A
-
kcat/Km is 2.2fold lower than the wild-type value
Y117A
-
kcat/Km is 5.8fold lower than the wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team