Transfer reactions catalyzed by β-D-xylosidase from Penicillium wortmanni

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Abstract
The .beta.-D-xylosidase from P. wortmanni catalyzes the hydrolysis of .beta.-D-xylopyranosides and .alpha.-L-arabinopyranosides, the transfer of the corresponding glycosyl residue to alcohols and the dismutation of aryl .beta.-D-xylopyranoside substrates. These reactions all occur with retention of configuration and can be rationalized by a symmetrical reaction scheme. The key intermediate is an enzyme-glycosyl complex with a lifetime that is sufficient for the diffusion away of the leaving (aglycon) group and the binding of an acceptor group before water reacts with the intermediate. The exact nature of this complex is unknown, but it must contain an aglycon site which binds preferentially alcohols and sugar molecules having the D-xylose structure.