Values CatLog read from this paper
Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional…
PMID 15799715doi:10.1042/bj20050167Open in Browse
The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.
CatLog read 4 records (7 values) from this paper: xylose reductase (AKR2B5) from Candida tenuis.
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks. CatLog calculated the 1 kcat/Km value marked “calc.” from kcat and Km; no printed kcat/Km was read for that record.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| xylose reductase (AKR2B5)variant D46N/K80A | Candida tenuis | D-xylose | — | — | 1.06 × 10⁻⁵ | pH 7, 25 °C | Open record: xylose reductase (AKR2B5) variant D46N/K80A, D-xylose |
| xylose reductase (AKR2B5)variant K80A | Candida tenuis | D-xyloseNADH constant and saturating (230 µM); D-xylose varied | 0.0017 | 1818 | 9.4 × 10⁻⁷ | pH 7, 25 °C | Open record: xylose reductase (AKR2B5) variant K80A, D-xylose |
| xylose reductase (AKR2B5)variant K80A | Candida tenuis | D-xyloseconstant ionic strength 0.61 M (NaCl); 230 µM NADH | 0.1 | 1.43 × 10³ | 7.0 × 10⁻⁵ calc. | pH 7, 25 °C | Open record: xylose reductase (AKR2B5) variant K80A, D-xylose |
| xylose reductase (AKR2B5)variant K80A | Candida tenuis | xylitol | — | — | 2.9 × 10⁻⁹ | pH 7, 25 °C | Open record: xylose reductase (AKR2B5) variant K80A, xylitol |