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 Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
- |
Candida parapsilosis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Candida parapsilosis | Q76L37 | - |
- |
Candida parapsilosis IFO 0708 | Q76L37 | - |
- |
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 | 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 | 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 | 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 | 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 |