Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.
    Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH (2013), Proteins, 81, 2059-2063.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.358 expressed in Escherichia coli Rosetta(DE3) cells Candida parapsilosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.214 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, 20°C, 2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement and modeling Candida parapsilosis
1.1.1.358 sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 25% (w/v) PEG3350, and 0.2 M NaCl Candida parapsilosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.214 35000
-
-
 Candida parapsilosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.214 (R)-pantolactone + NADP+ Candida parapsilosis
-
 2-dehydropantolactone + NADPH + H+
-
 r
1.1.1.214 (R)-pantolactone + NADP+ Candida parapsilosis IFO 0708
-
 2-dehydropantolactone + NADPH + H+
-
 r
1.1.1.214 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
1.1.1.214 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
1.1.1.358 2-dehydropantolactone + NADPH + H+ Candida parapsilosis
-
 (R)-pantolactone + NADP+
-
 ?
1.1.1.358 2-dehydropantolactone + NADPH + H+ Candida parapsilosis IFO 0708
-
 (R)-pantolactone + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.214 Candida parapsilosis Q76L37
-
-
1.1.1.214 Candida parapsilosis IFO 0708 Q76L37
-
-
1.1.1.358 Candida parapsilosis Q76L36
-
-
1.1.1.358 Candida parapsilosis IFO 0708 Q76L36
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.358 Ni Sepharose column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration Candida parapsilosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.214 (R)-pantolactone + NADP+
-
 Candida parapsilosis 2-dehydropantolactone + NADPH + H+
-
 r
1.1.1.214 (R)-pantolactone + NADP+
-
 Candida parapsilosis IFO 0708 2-dehydropantolactone + NADPH + H+
-
 r
1.1.1.214 2-dehydropantolactone + NADPH + H+ the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner Candida parapsilosis (R)-pantolactone + NADP+
-
 r
1.1.1.214 2-dehydropantolactone + NADPH + H+ the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner. Candida parapsilosis (R)-pantolactone + NADP+
-
 r
1.1.1.214 2-dehydropantolactone + NADPH + H+ the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner Candida parapsilosis IFO 0708 (R)-pantolactone + NADP+
-
 r
1.1.1.214 2-dehydropantolactone + NADPH + H+ the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner. Candida parapsilosis IFO 0708 (R)-pantolactone + NADP+
-
 r
1.1.1.214 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 Candida parapsilosis ?
-
 ?
1.1.1.214 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 Candida parapsilosis IFO 0708 ?
-
 ?
1.1.1.358 2-dehydropantolactone + NADPH + H+
-
 Candida parapsilosis (R)-pantolactone + NADP+
-
 ?
1.1.1.358 2-dehydropantolactone + NADPH + H+
-
 Candida parapsilosis IFO 0708 (R)-pantolactone + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.214 ? x * 35000, about, sequence calculation Candida parapsilosis
1.1.1.214 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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.214 conjugated polyketone reductase
-
 Candida parapsilosis
1.1.1.214 CPR-C1
-
 Candida parapsilosis
1.1.1.214 NADPH-dependent conjugated polyketone reductase
-
 Candida parapsilosis
1.1.1.214 NADPH-dependent ketopantoyl lactone reductase
-
 Candida parapsilosis
1.1.1.358 conjugated polyketone reductase
-
 Candida parapsilosis
1.1.1.358 CPR-C1
-
 Candida parapsilosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.214 NADP+
-
 Candida parapsilosis
1.1.1.214 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
1.1.1.358 NADPH dependent on Candida parapsilosis

General Information

EC Number General Information Comment Organism
1.1.1.214 evolution the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily Candida parapsilosis
1.1.1.214 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