BRENDA - Enzyme Database show
show all sequences of 1.1.1.214

Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH

Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.; Proteins 81, 2059-2063 (2013)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
purified enzyme in complex with NADPH, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM NADPH, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 25% w/v PEG 3350, and 0.2 M NaCl, 20C, 2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement and modeling
Candida parapsilosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
-
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 + H+
-
-
r
(R)-pantolactone + NADP+
Candida parapsilosis IFO 0708
-
2-dehydropantolactone + NADPH + H+
-
-
r
2-dehydropantolactone + NADPH + H+
Candida parapsilosis
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
(R)-pantolactone + NADP+
-
-
r
2-dehydropantolactone + NADPH + H+
Candida parapsilosis IFO 0708
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
(R)-pantolactone + NADP+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Candida parapsilosis
Q76L37
-
-
Candida parapsilosis IFO 0708
Q76L37
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantolactone + NADP+
-
726465
Candida parapsilosis
2-dehydropantolactone + NADPH + H+
-
-
-
r
(R)-pantolactone + NADP+
-
726465
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH + H+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
726465
Candida parapsilosis
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
726465
Candida parapsilosis
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
726465
Candida parapsilosis IFO 0708
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
726465
Candida parapsilosis IFO 0708
(R)-pantolactone + NADP+
-
-
-
r
additional information
the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
726465
Candida parapsilosis
?
-
-
-
-
additional information
the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
726465
Candida parapsilosis IFO 0708
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 35000, about, sequence calculation
Candida parapsilosis
More
CPR-C1 has 12 alpha-helices, 10 beta-strands, and five 310-helices, and adopts a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH
Candida parapsilosis
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Candida parapsilosis
NADPH
CPR-C1 has a conserved GXGTX motif, but a binding mode for recognizing the adenosine 2'-phosphate group of NADPH, binding structure, overview
Candida parapsilosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Candida parapsilosis
NADPH
CPR-C1 has a conserved GXGTX motif, but a binding mode for recognizing the adenosine 2'-phosphate group of NADPH, binding structure, overview
Candida parapsilosis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified enzyme in complex with NADPH, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM NADPH, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 25% w/v PEG 3350, and 0.2 M NaCl, 20C, 2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement and modeling
Candida parapsilosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
-
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 + H+
-
-
r
(R)-pantolactone + NADP+
Candida parapsilosis IFO 0708
-
2-dehydropantolactone + NADPH + H+
-
-
r
2-dehydropantolactone + NADPH + H+
Candida parapsilosis
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
(R)-pantolactone + NADP+
-
-
r
2-dehydropantolactone + NADPH + H+
Candida parapsilosis IFO 0708
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
(R)-pantolactone + NADP+
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantolactone + NADP+
-
726465
Candida parapsilosis
2-dehydropantolactone + NADPH + H+
-
-
-
r
(R)-pantolactone + NADP+
-
726465
Candida parapsilosis IFO 0708
2-dehydropantolactone + NADPH + H+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
726465
Candida parapsilosis
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
726465
Candida parapsilosis
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
726465
Candida parapsilosis IFO 0708
(R)-pantolactone + NADP+
-
-
-
r
2-dehydropantolactone + NADPH + H+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
726465
Candida parapsilosis IFO 0708
(R)-pantolactone + NADP+
-
-
-
r
additional information
the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
726465
Candida parapsilosis
?
-
-
-
-
additional information
the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
726465
Candida parapsilosis IFO 0708
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 35000, about, sequence calculation
Candida parapsilosis
More
CPR-C1 has 12 alpha-helices, 10 beta-strands, and five 310-helices, and adopts a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH
Candida parapsilosis
General Information
General Information
Commentary
Organism
evolution
the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
Candida parapsilosis
additional information
CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH. Homology structure modeling, overview
Candida parapsilosis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
Candida parapsilosis
additional information
CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH. Homology structure modeling, overview
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)
724098
Qin
Structure of conjugated polyke ...
Candida parapsilosis, Candida parapsilosis IFO 0708
Appl. Microbiol. Biotechnol.
98
243-249
2013
-
-
1
1
11
-
-
-
-
-
-
4
-
6
-
-
1
-
-
-
1
-
6
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
11
-
-
-
-
-
-
-
-
4
-
-
-
1
-
-
1
-
6
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726465
Qin
Crystal structure of conjugate ...
Candida parapsilosis, Candida parapsilosis IFO 0708
Proteins
81
2059-2063
2013
-
-
-
1
-
-
-
-
-
-
1
4
-
4
-
-
-
-
-
-
-
-
8
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
4
-
-
-
-
-
-
-
-
8
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
654311
Kataoka
Gene cloning and overexpressio ...
Candida parapsilosis, Candida parapsilosis IFO 0708
Appl. Microbiol. Biotechnol.
64
359-366
2004
-
1
1
-
-
-
1
-
-
-
2
2
-
11
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-