BRENDA - Enzyme Database show
show all sequences of 1.6.5.10

Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine

Schlegel, B.P.; Ratnam, K.; Penning, T.M.; Biochemistry 37, 11003-11011 (1998)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
D50N
less than 0.1% of wild-type activity
Rattus norvegicus
H117A
less than 0.1% of wild-type activity
Rattus norvegicus
K84M
complete loss of activity
Rattus norvegicus
K84R
complete loss of activity
Rattus norvegicus
Y55F
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Rattus norvegicus
Y55S
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
0.012
-
9,10-phenanthrenequinone
mutant D50E, pH 6.0, 25C
Rattus norvegicus
0.014
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.026
-
9,10-phenanthrenequinone
mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.044
-
9,10-phenanthrenequinone
mutant H117A, pH 6.0, 25C
Rattus norvegicus
0.056
-
9,10-phenanthrenequinone
mutant D50N, pH 6.0, 25C
Rattus norvegicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
P23457
-
-
Renatured (Commentary)
Commentary
Organism
-
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.000003
-
substrate (R,S)-camphorquinone, mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.00002
-
substrate (R,S)-camphorquinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0006
-
substrate acenaphthenequinone, mutant Y55F, pH 6.0, 25C; substrate acenaphthenequinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0016
-
substrate 9,10-phenanthrenenquinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0018
-
substrate 9,10-phenanthrenenquinone, mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.0025
-
substrate (R,S)-camphorquinone, wild-type, pH 6.0, 25C
Rattus norvegicus
0.0038
-
substrate acenaphthenequinone, wild-type, pH 6.0, 25C
Rattus norvegicus
0.0044
-
substrate 9,10-phenanthrenenquinone, wild-type, pH 6.0, 25C
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-camphorquinone + NADPH + H+
-
714140
Rattus norvegicus
(R,S)-camphorquinone + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
-
714140
Rattus norvegicus
9,10-phenanthrenequinol + NADP+
-
-
-
?
acenaphthenequinone + NADPH + H+
-
714140
Rattus norvegicus
acenaphthenequinol + NADP+
-
-
-
?
additional information
enzyme displays bifunctional 3alpha-hydroxysteroid dehydrogenase and NADPH reductase (quinone) activities. Quinone reduction occurs via a mechanism that differs from 3-ketosteroid reduction. In this mechanism, the electron donor NADPH and acceptor o-quinone are bound in close proximity, which permits hydride transfer without formal protonation of the acceptor carbonyl by Tyr 55
714140
Rattus norvegicus
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.01
-
9,10-phenanthrenequinone
mutant D50N, pH 6.0, 25C
Rattus norvegicus
0.02
-
9,10-phenanthrenequinone
mutant D50E, pH 6.0, 25C
Rattus norvegicus
0.04
-
9,10-phenanthrenequinone
mutant H117A, pH 6.0, 25C
Rattus norvegicus
1.45
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C; mutant Y55S, pH 6.0, 25C
Rattus norvegicus
2.85
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the pH dependency of 9,10-phenanthrenequinone reduction catalyzed by the wild-type enzyme is different to that observed for 3-ketosteroid reduction. The kcat value for 9,10-phenanthrenequinone reduction is pH-dependent with the maximal rate decreasing with increasing pH but reveals an ionizable group with a pKb of 8.90 that must be protonated for maximal activity
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Rattus norvegicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D50N
less than 0.1% of wild-type activity
Rattus norvegicus
H117A
less than 0.1% of wild-type activity
Rattus norvegicus
K84M
complete loss of activity
Rattus norvegicus
K84R
complete loss of activity
Rattus norvegicus
Y55F
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Rattus norvegicus
Y55S
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
0.012
-
9,10-phenanthrenequinone
mutant D50E, pH 6.0, 25C
Rattus norvegicus
0.014
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.026
-
9,10-phenanthrenequinone
mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.044
-
9,10-phenanthrenequinone
mutant H117A, pH 6.0, 25C
Rattus norvegicus
0.056
-
9,10-phenanthrenequinone
mutant D50N, pH 6.0, 25C
Rattus norvegicus
Renatured (Commentary) (protein specific)
Commentary
Organism
-
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.000003
-
substrate (R,S)-camphorquinone, mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.00002
-
substrate (R,S)-camphorquinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0006
-
substrate acenaphthenequinone, mutant Y55F, pH 6.0, 25C; substrate acenaphthenequinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0016
-
substrate 9,10-phenanthrenenquinone, mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.0018
-
substrate 9,10-phenanthrenenquinone, mutant Y55F, pH 6.0, 25C
Rattus norvegicus
0.0025
-
substrate (R,S)-camphorquinone, wild-type, pH 6.0, 25C
Rattus norvegicus
0.0038
-
substrate acenaphthenequinone, wild-type, pH 6.0, 25C
Rattus norvegicus
0.0044
-
substrate 9,10-phenanthrenenquinone, wild-type, pH 6.0, 25C
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-camphorquinone + NADPH + H+
-
714140
Rattus norvegicus
(R,S)-camphorquinone + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
-
714140
Rattus norvegicus
9,10-phenanthrenequinol + NADP+
-
-
-
?
acenaphthenequinone + NADPH + H+
-
714140
Rattus norvegicus
acenaphthenequinol + NADP+
-
-
-
?
additional information
enzyme displays bifunctional 3alpha-hydroxysteroid dehydrogenase and NADPH reductase (quinone) activities. Quinone reduction occurs via a mechanism that differs from 3-ketosteroid reduction. In this mechanism, the electron donor NADPH and acceptor o-quinone are bound in close proximity, which permits hydride transfer without formal protonation of the acceptor carbonyl by Tyr 55
714140
Rattus norvegicus
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.01
-
9,10-phenanthrenequinone
mutant D50N, pH 6.0, 25C
Rattus norvegicus
0.02
-
9,10-phenanthrenequinone
mutant D50E, pH 6.0, 25C
Rattus norvegicus
0.04
-
9,10-phenanthrenequinone
mutant H117A, pH 6.0, 25C
Rattus norvegicus
1.45
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C; mutant Y55S, pH 6.0, 25C
Rattus norvegicus
2.85
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the pH dependency of 9,10-phenanthrenequinone reduction catalyzed by the wild-type enzyme is different to that observed for 3-ketosteroid reduction. The kcat value for 9,10-phenanthrenequinone reduction is pH-dependent with the maximal rate decreasing with increasing pH but reveals an ionizable group with a pKb of 8.90 that must be protonated for maximal activity
Rattus norvegicus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.06
-
9,10-phenanthrenequinone
mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.1
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C
Rattus norvegicus
1.43
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.06
-
9,10-phenanthrenequinone
mutant Y55S, pH 6.0, 25C
Rattus norvegicus
0.1
-
9,10-phenanthrenequinone
mutant Y55F, pH 6.0, 25C
Rattus norvegicus
1.43
-
9,10-phenanthrenequinone
wild-type, pH 6.0, 25C
Rattus norvegicus
Other publictions for EC 1.6.5.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743650
Brissos
Improving kinetic or thermody ...
Pseudomonas putida, Pseudomonas putida MET94
PLoS ONE
9
e87209
2014
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21
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1
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7
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12
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21
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12
1
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1
1
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724333
Hervas
ArsH from the cyanobacterium S ...
Synechocystis sp.
Biochemistry
51
1178-1187
2012
-
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1
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2
9
-
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1
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1
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1
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10
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1
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7
1
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1
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2
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9
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1
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10
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1
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7
1
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4
4
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714708
Crosas
Novel alkenal/one reductase ac ...
Saccharomyces cerevisiae
Chem. Biol. Interact.
191
32-37
2011
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1
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1
2
2
701035
Zai
Oxidative stress in tardive dy ...
Homo sapiens
Prog. Neuropsychopharmacol. Biol. Psychiatry
34
50-56
2009
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688840
Hong
The NADPH quinone reductase Md ...
Helicobacter hepaticus, Helicobacter hepaticus ATCC 51449
Microb. Pathog.
44
169-174
2008
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1
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690177
Huang
Arsenic methylation capability ...
Homo sapiens
Urol. Int.
80
405-412
2008
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695605
Wagner
The natural compound ascorbige ...
Rattus norvegicus
Ann. Nutr. Metab.
53
122-128
2008
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4
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696015
Endo
Human carbonyl reductase 4 is ...
Homo sapiens
Biochem. Biophys. Res. Commun.
377
1326-1330
2008
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1
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4
9
1
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2
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4
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10
1
1
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7
1
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1
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3
9
1
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10
1
1
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1
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699129
Lambertucci
Palmitate increases superoxide ...
Rattus norvegicus
J. Cell. Physiol.
216
796-804
2008
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699999
Laurindo
Assessment of superoxide produ ...
Homo sapiens
Methods Enzymol.
441
237-260
2008
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1
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688593
Gharavi
Role of nitric oxide in downre ...
Mus musculus
J. Pharm. Sci.
96
2795-2807
2007
1
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674461
Kitzing
The 1.3 A crystal structure of ...
Bacillus subtilis
J. Biol. Chem.
280
27904-27913
2005
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658899
Wang
An NADPH quinone reductase of ...
Helicobacter pylori
Infect. Immun.
72
1391-1396
2004
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