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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types.

Starting from a common tyrosine, yeast xylose reductases (XRs) contain two conserved sequence motifs corresponding to the catalytic signatures of single-domain reductases/epimerases/dehydrogenases (Tyr(n)-(X)3-Lys(n+4)) and aldo/keto reductases (AKRs) (Tyr(n)-(X)28-Lys(n+29)). Tyr(51), Lys(55) and Lys(80) of XR from Candida tenuis were replaced by site-directed mutagenesis. The purified Tyr(51)--> Phe and Lys(80)-->Ala mutants showed turnover numbers and catalytic efficiencies for NADH-dependent reduction of D-xylose between 2500- and 5000-fold below wild-type levels, suggesting a catalytic role of both residues. Replacing Lys(55) by Asn, a substitution found in other AKRs, did not detectably affect binding of coenzymes, and enzymatic catalysis to carbonyl/alcohol interconversion. The contribution of Tyr(51) to rate enhancement of aldehyde reduction conforms with expectations for the general acid catalyst of the enzymatic reaction.[1]

References

  1. Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types. Klimacek, M., Szekely, M., Griessler, R., Nidetzky, B. FEBS Lett. (2001) [Pubmed]
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