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

BRENDA support

1.1.1.214: 2-dehydropantolactone reductase (Si-specific)

This is an abbreviated version!
For detailed information about 2-dehydropantolactone reductase (Si-specific), go to the full flat file.

Word Map on EC 1.1.1.214

Reaction

(R)-pantolactone
+
NADP+
=
2-dehydropantolactone
 +
NADPH
 +
H+

Synonyms

2-dehydropantoyl-lactone reductase (B-specific), 2-ketopantoyl lactone reductase, 2-oxopantoyl lactone reductase, conjugated polyketone reductase, conjugated polyketone reductase C2, CORT_0G03830, CPR, CPR-C1, CPR-C2, ketopantoyl lactone reductase, NADPH-dependent conjugated polyketone reductase, NADPH-dependent ketopantoyl lactone reductase, nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.214 2-dehydropantolactone reductase (Si-specific)

Crystallization

Crystallization on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and docking analysis. Structure reveals a triosephosphate isomerase barrel fold comprised of eight beta-strands and eight alpha-helices
purified enzyme in apoform and in complex with NADPH, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution consisting of 0.1 M Tris-HCl, pH 8.1, and 23% w/v PEG 3350 at 20°C, for the enzyme-NADPH complexed crystals, the protein in 20 mM Tris-HCl, pH 8.0, and 5 mM MADPH, is mixed with 0.1 M Tris–HCl, pH 7.4, and 256% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.70 A and 1.80 A resolution, respectively, molecular replacement method
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