BRENDA - Enzyme Database show
show all sequences of 1.6.5.10

Novel alkenal/one reductase activity of yeast NADPH:quinone reductase Zta1p. Prospect of the functional role for the zeta-crystallin family

Crosas, E.; Porte, S.; Moeini, A.; Farres, J.; Biosca, J.A.; Pares, X.; Fernandez, M.R.; Chem. Biol. Interact. 191, 32-37 (2011)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
0.009
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-naphthoquinone + NADPH + H+
-
714708
Saccharomyces cerevisiae
1,2-naphthoquinol + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
-
714708
Saccharomyces cerevisiae
9,10-phenanthrenequinol + NADP+
-
-
-
?
additional information
trace activity with substrates acrolein, cinnamaldehyde, 3-buten-2-one, 3-penten-2-one, 3-nonen-2-one
714708
Saccharomyces cerevisiae
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.2
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
4.2
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
0.009
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-naphthoquinone + NADPH + H+
-
714708
Saccharomyces cerevisiae
1,2-naphthoquinol + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
-
714708
Saccharomyces cerevisiae
9,10-phenanthrenequinol + NADP+
-
-
-
?
additional information
trace activity with substrates acrolein, cinnamaldehyde, 3-buten-2-one, 3-penten-2-one, 3-nonen-2-one
714708
Saccharomyces cerevisiae
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.2
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
4.2
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
Expression
Organism
Commentary
Expression
Saccharomyces cerevisiae
induction under different types of cellular stress, including ethanol and dimethylsulfoxide exposure and by reaching the stationary growth phase
up
General Information
General Information
Commentary
Organism
physiological function
presence of Zta1p has an in vivo protective effect on yeast strains exposed to the toxic substrate 3-penten-2-one
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
presence of Zta1p has an in vivo protective effect on yeast strains exposed to the toxic substrate 3-penten-2-one
Saccharomyces cerevisiae
Expression (protein specific)
Organism
Commentary
Expression
Saccharomyces cerevisiae
induction under different types of cellular stress, including ethanol and dimethylsulfoxide exposure and by reaching the stationary growth phase
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
462
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
1041
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
462
-
1,2-naphthoquinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
1041
-
9,10-phenanthrenequinone
pH 7.0, temperature not specified in the publication
Saccharomyces cerevisiae
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
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2014
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1
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21
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1
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7
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1
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21
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1
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12
1
1
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1
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1
1
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-
724333
Hervas
ArsH from the cyanobacterium S ...
Synechocystis sp.
Biochemistry
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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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10
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7
1
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1
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9
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10
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1
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7
1
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4
4
-
-
-
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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3
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2
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1
1
1
1
2
2
701035
Zai
Oxidative stress in tardive dy ...
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Hong
The NADPH quinone reductase Md ...
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6
1
1
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1
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696015
Endo
Human carbonyl reductase 4 is ...
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Biochem. Biophys. Res. Commun.
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2008
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9
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10
1
1
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7
1
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1
3
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1
1
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4
3
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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-
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1
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1
1
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-
699999
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Assessment of superoxide produ ...
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1
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1
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1
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1
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1
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2
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658899
Wang
An NADPH quinone reductase of ...
Helicobacter pylori
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13
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2
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1
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13
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655940
Kim
Molecular cloning and characte ...
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1
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1
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714140
Schlegel
Retention of NADPH-linked quin ...
Rattus norvegicus
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6
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6
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1
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6
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1
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4
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1
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Diatchuk
Inhibition of NADPH oxidase ac ...
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1
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Hayashi
NADPH-specific quinone reducta ...
Escherichia coli
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1996
1
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Batot
Characterization of neutrophil ...
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Viljoen
-
Isolation and characterization ...
Microcystis aeruginosa
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1985
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6
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392827
Pupillo
-
Pyridine nucleotide-linked deh ...
Cucurbita pepo, Zea mays
Dev. Plant Biol.
7
321-328
1982
-
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392826
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Purification and properties of ...
Sus scrofa
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1
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392782
Jagendorf
-
Chloroplast TPNH diaphorase ...
Spinacia oleracea
Methods Enzymol.
6
430-434
1963
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6
1
1
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1
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1
1
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9
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-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
6
-
1
1
-
1
-
-
-
-
-
-
1
1
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-