Information on EC 1.1.1.B57 - 1-tetralone reductase [NADPH]

for references in articles please use BRENDA:EC1.1.1.B57
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.B57
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
1-tetralone reductase [NADPH]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-tetralone + NADPH + H+ = 1-tetralol + NADP+
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
1-tetralol:NADP+ oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
(R)-scytalone + NADP+
show the reaction diagram
1,3,8-trihydroxynaphthalene + NADPH + H+
(R)-vermelone + NADP+
show the reaction diagram
1-indanone + NADPH + H
3-hydroxy-1-indanone + NADP+
show the reaction diagram
1-tetralone + NADPH + H
(S)-4-hydroxy-1-tetralone + NADP+
show the reaction diagram
1-tetralone + NADPH + H+
1-tetralol + NADP+
show the reaction diagram
2,3-dihydronaphthalene-14-dione + NADPH + H+
(S)-4-hydroxy-1-tetralone + NADP+
show the reaction diagram
2,3-epoxy-1,4-naphthoquinone + NADPH + H+
(1aS,7R,7aS)-7-hydroxy-7,7a-dihydronaphtho[2,3-b]oxiren-2(1aH)-one + NADP+
show the reaction diagram
2-hydroxy-1,4-naphthoquinone + 2 NADPH + H+
(3S,4R)-3,4-dihydroxy-1-tetralone + 2 NADP+
show the reaction diagram
i.e. lawsone, enzyme T4HNR exhibits high diastereoselectivity (cis/trans99:1), high enantiomeric excess (over 99% ee), and 90% yield. The putative two-step enzymatic formation of cis-ketodiol from 2-hydroxyquinone lawsone does not involve the hydroquinone. Stable 1,4-diketo tautomer intermediate
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-
?
2-hydroxy-1,4-naphthoquinone + NADPH + H+
cis-3,4-dihydroxy-1-tetralone + NADP+
show the reaction diagram
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-
-
?
3,4-dihydro-1(2H)-naphthalenone + NADPH + H+
1,2,3,4-tetrahydronaphthalen-1-ol + NADP+
show the reaction diagram
5-hydroxy-2,3-dihydronaphthalene-1,4-dione + NADPH + H+
(S)-4,8-dihydroxy-1-tetralone + NADP+
show the reaction diagram
-
-
-
?
5-methoxy-1-tetralone + NADPH + H
(S)-4-hydroxy-5-methoxy-1-tetralone + NADP+
show the reaction diagram
6-methoxy-1-tetralone + NADPH + H
(S)-4-hydroxy-6-methoxy-1-tetralone + NADP+
show the reaction diagram
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-
-
?
flaviolin + NADPH + H+
cis-(3S,4R)-4-hydroxyscytalone + NADP+
show the reaction diagram
-
-
-
?
indane + NADPH + H+
(S)-4-hydroxy-indan + NADP+
show the reaction diagram
tetralin + NADPH + H+
(S)-4-hydroxy-tetralin + NADP+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
(R)-scytalone + NADP+
show the reaction diagram
1,3,8-trihydroxynaphthalene + NADPH + H+
(R)-vermelone + NADP+
show the reaction diagram
indane + NADPH + H+
(S)-4-hydroxy-indan + NADP+
show the reaction diagram
tetralin + NADPH + H+
(S)-4-hydroxy-tetralin + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
important for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-[2-(diphenylmethoxy)ethyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
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i.e. GBR12783
1-[2-[bis(4-fluorophenyl)methoxy]ethyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
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1-[bis(4-fluorophenyl)methyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
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i.e. flunarizine
EDTA
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1 mM, 20% decrease in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
3,4-dihydro-1(2H)-naphthalenone
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95C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1719
3,4-dihydro-1(2H)-naphthalenone
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95C, pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
1-[2-(diphenylmethoxy)ethyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
Pyrobaculum aerophilum
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pH 7.5, 37C
0.01
1-[2-[bis(4-fluorophenyl)methoxy]ethyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
Pyrobaculum aerophilum
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pH 7.5, 37C
0.04
1-[bis(4-fluorophenyl)methyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
Pyrobaculum aerophilum
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pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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60C, pH 7.5
50
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95C, pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
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reaction rate increases with temperature up to 95C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38580
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x * 38580, calculated from sequence
40000
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x * 40000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of both wild-type and cobalt-substituted enzyme at 1.75 A and 2.20 A resolution, respectively. One metal ion per monomer is present only at the structural site. The co-crystal structure of the NADPH-bound form of the enzyme at 2.35 A resolution shows close structural conservation with horse ADH, despite the lack of a catalytic Zn2+. Modeling of 1-tetralone into the NADPH-bound structure suggests an arginine as a possible catalytic residue
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Zn2+ is not essential for structural stability of the enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A328F
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328K
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328R
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328Y
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328F
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site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
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A328K
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site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
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A328R
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site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
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A328Y
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site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis