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show all sequences of 1.1.1.214

Gene cloning and overexpression of two conjugated polyketone reductases, novel aldo-keto reductase family enzymes, of Candida parapsilosis. Investigation of hydroxamic acids as laccase-mediators for pulp bleaching

Kataoka, M.; Delacruz-Hidalgo, A.R.G.; Akond, M.A.; Sakuradani, E.; Kita, K.; Shimizu, S.; Appl. Microbiol. Biotechnol. 64, 359-366 (2004)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
enzyme is useful for production of chiral alcohols
Candida parapsilosis
Cloned(Commentary)
Commentary
Organism
isozyme CPR-C2, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme; isozymes CPR-C1, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme
Candida parapsilosis
Inhibitors
Inhibitors
Commentary
Organism
Structure
(R)-pantolactone
substrate inhibition of the recombinant isozyme expressed in Escherichia coli at a concentration above 10 mg/ml
Candida parapsilosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, recombinant isozyme CPR-C2, SDS-PAGE
Candida parapsilosis
38000
-
x * 38000, recombinant isozyme CPR-C1, SDS-PAGE
Candida parapsilosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantolactone + NADP+
Candida parapsilosis
-
2-dehydropantolactone + NADPH
-
-
?
(R)-pantolactone + NADP+
Candida parapsilosis IFO 0708
-
2-dehydropantolactone + NADPH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Candida parapsilosis
Q76L36
isozyme CPR-C2; strain IFO 0708, 2 isozymes CPR-C1 and CPR-C2
-
Candida parapsilosis
Q76L37
isozyme CPR-C1; strain IFO 0708, 2 isozymes CPR-C1 and CPR-C2
-
Candida parapsilosis IFO 0708
Q76L36
isozyme CPR-C2; strain IFO 0708, 2 isozymes CPR-C1 and CPR-C2
-
Candida parapsilosis IFO 0708
Q76L37
isozyme CPR-C1; strain IFO 0708, 2 isozymes CPR-C1 and CPR-C2
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
5.03
-
recombinant isozyme CPR-C2 in cell extract of expressing Escherichia coli cells in absence of IPTG
Candida parapsilosis
19.3
-
recombinant isozyme CPR-C1 in cell extract of expressing Escherichia coli cells in absence of IPTG
Candida parapsilosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantolactone + NADP+
-
654311
Candida parapsilosis
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
i.e. ketopantoyl lactone
654311
Candida parapsilosis
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
i.e. ketopantoyl lactone
654311
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
-
654311
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 36000, recombinant isozyme CPR-C2, SDS-PAGE; x * 38000, recombinant isozyme CPR-C1, SDS-PAGE
Candida parapsilosis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
28
-
assay at
Candida parapsilosis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
about
Candida parapsilosis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
9
-
Candida parapsilosis
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Candida parapsilosis
Application (protein specific)
Application
Commentary
Organism
synthesis
enzyme is useful for production of chiral alcohols
Candida parapsilosis
Cloned(Commentary) (protein specific)
Commentary
Organism
isozyme CPR-C2, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme; isozymes CPR-C1, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme
Candida parapsilosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Candida parapsilosis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(R)-pantolactone
substrate inhibition of the recombinant isozyme expressed in Escherichia coli at a concentration above 10 mg/ml
Candida parapsilosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, recombinant isozyme CPR-C2, SDS-PAGE
Candida parapsilosis
38000
-
x * 38000, recombinant isozyme CPR-C1, SDS-PAGE
Candida parapsilosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantolactone + NADP+
Candida parapsilosis
-
2-dehydropantolactone + NADPH
-
-
?
(R)-pantolactone + NADP+
Candida parapsilosis IFO 0708
-
2-dehydropantolactone + NADPH
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
5.03
-
recombinant isozyme CPR-C2 in cell extract of expressing Escherichia coli cells in absence of IPTG
Candida parapsilosis
19.3
-
recombinant isozyme CPR-C1 in cell extract of expressing Escherichia coli cells in absence of IPTG
Candida parapsilosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantolactone + NADP+
-
654311
Candida parapsilosis
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
i.e. ketopantoyl lactone
654311
Candida parapsilosis
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
i.e. ketopantoyl lactone
654311
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
-
654311
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 36000, recombinant isozyme CPR-C2, SDS-PAGE; x * 38000, recombinant isozyme CPR-C1, SDS-PAGE
Candida parapsilosis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
28
-
assay at
Candida parapsilosis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
about
Candida parapsilosis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
9
-
Candida parapsilosis
Other publictions for EC 1.1.1.214
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)
654311
Kataoka
Gene cloning and overexpressio ...
Candida parapsilosis, Candida parapsilosis IFO 0708
Appl. Microbiol. Biotechnol.
64
359-366
2004
-
1
1
-
-
-
1
-
-
-
2
2
-
10
-
-
-
-
-
-
2
-
4
1
1
-
-
-
1
1
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
-
-
2
2
-
-
-
-
-
-
2
-
4
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
347731
Julliard
-
Purification and characterizat ...
Spinacia oleracea
Bot. Acta
107
191-200
1994
-
-
-
-
-
-
2
-
1
-
1
1
-
1
-
-
1
-
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
1
1
-
-
-
1
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286105
Wilken
Ketopantoic acid and ketopanto ...
Escherichia coli
J. Biol. Chem.
250
2311-2314
1975
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-