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1.1.1.307: D-xylose reductase [NAD(P)H]

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

Word Map on EC 1.1.1.307

Reaction

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

Synonyms

AKR2B5, ALR2, CTHT_0056950, CtXR, dsXR, dual specific xylose reductase, KmXYL1, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent D-xylose reductase-like protein, NAD(P)H-dependent XR, NAD(P)H-dependent xylose reductase, NAD(P)H-linked xylose reductase, NADH/NADPH-xylose reductase, NADP-dependent xylose reductase, PsXR, PsXYL1, SaXYL1, SpXYL1.1, SsXR, Texr, XR, XYL1, xylose reductase, XylR, XyrA

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.307 D-xylose reductase [NAD(P)H]

Renatured

Renatured on EC 1.1.1.307 - D-xylose reductase [NAD(P)H]

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation buffers of either pH 6.0 or 8.0, containing urea in concentrations of 2, 4, 6, and 8 M, are used and analysed in SDS-PAGE. Optimal solvation of the XylR giving the lowest background of Escherichia coli proteins is performed with 4 M urea at pH 8.0. For renaturation, a set of buffers containing 0, 0.1, 0.5, 1 and 1.5 mM glutathione (red:ox = 1:1) at pH values of 5.0, 6.0, 7.0, and 8.0 are tested. Refolding occurrs at 8°C and its progress is analysed by assaying the volumetric activity in the respective buffers. Best renaturation results are obtained in a 20 mM Tris/HCl buffer at pH 7.0 without glutathione. After 4 days about 70% of the activity of the XylR is recovered. Buffers at pH 8.0 work slightly less efficient compared to that of pH 7.0. At pH 5.0 and 6.0 refolding is drastically reduced. Increasing concentrations of glutathione do not improve renaturation