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Literature summary for 1.1.1.214 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

Crystallization (Commentary)

Crystallization (Comment) 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, 20°C, 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] Comment Organism
35000
-
-
Candida parapsilosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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 UniProt Comment Textmining
Candida parapsilosis Q76L37
-
-
Candida parapsilosis IFO 0708 Q76L37
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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+ the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner 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. 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 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. 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 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 Candida parapsilosis IFO 0708 ?
-
?

Subunits

Subunits Comment 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

Synonyms

Synonyms Comment Organism
conjugated polyketone reductase
-
Candida parapsilosis
CPR-C1
-
Candida parapsilosis
NADPH-dependent conjugated polyketone reductase
-
Candida parapsilosis
NADPH-dependent ketopantoyl lactone reductase
-
Candida parapsilosis

Cofactor

Cofactor Comment 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

General Information

General Information Comment 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