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1.1.1.431: D-xylose reductase (NADPH)

This is an abbreviated version!
For detailed information about D-xylose reductase (NADPH), go to the full flat file.

Reaction

xylitol
+
NAD(P)+
=
D-xylose
+
NAD(P)H
+
H+

Synonyms

ALR1, Cb-XR, CbXR, CtXR, D-xylose reductase, D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, DnXR, GRE3, monospecific xylose reductase, More, msXR, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent xylose reductase, NADPH dependent D-xylose reductase, NADPH-dependent D-xylose reductase II,III, NADPH-dependent xylose reductase, NADPH-preferring xylose reductase, NRRL3_10868, SsXR, Texr, TrxR, XR1, XR2, XR3, XRTL, XYL1, xylose reductase, xyr8, XyrA, XyrB

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.431 D-xylose reductase (NADPH)

pH Stability

pH Stability on EC 1.1.1.431 - D-xylose reductase (NADPH)

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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
purified recombinant wild-type and engineered enzymes have a half-life of 1.2 h
761007
5
purified recombinant wild-type enzyme has a half-life of 10 h, engineered enzyme Pir-XR of 30 h, and engineered enzyme XR-GPI of 30 h
761007
5 - 9
the purified recombinant enzyme exhibits remarkable stability at pH 6 and pH 7. It retains 58.7%, 73.76%, and 45.95% activity after 30 min at pH 5.0, pH 8.0, and pH 9.0, respectively. The activity at pH 5.0 and pH 8.0 declines to 27% and 54%, respectively, after an incubation of 60 min
760720
6
purified recombinant wild-type enzyme has a half-life of 5 h, engineered enzyme Pir-XR of 20 h, and engineered enzyme XR-GPI of 20 h
761007
additional information
alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time. The secondary structure of enzyme DnXR is completely affected at pH 5.0 and is retained at pH 5.5 with altered signature. Negative ellipticity values are reduced at pH 6.0 and 10.0 without alteration in secondary signatures. Overlapping spectra are obtained at pH 7.0, pH 8.0, and pH 9.0 with the highest signals. Effect of pH on thermodynamic parameters, overview
761017