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The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune
Author(s) -
Eis Christian,
Albert Martin,
Dax Karl,
Nidetzky Bernd
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01504-x
Subject(s) - schizophyllum commune , phosphorolysis , trehalose , chemistry , anomer , glycogen phosphorylase , stereospecificity , catalysis , protonation , fluoride , organic chemistry , stereochemistry , biochemistry , enzyme , inorganic chemistry , ion , purine nucleoside phosphorylase , purine
Phosphorolysis of α,α‐trehalose catalyzed by trehalose phosphorylase from the basidiomycete Schizophyllum commune proceeds via net retention of anomeric configuration and yields α‐ d ‐glucose 1‐phosphate and α‐ d ‐glucose as the products. In reverse reaction, only the α‐anomers of d ‐glucose 1‐phosphate and d ‐glucose are utilized as glucosyl donor and acceptor, respectively, and give exclusively the α,α‐product. Trehalose phosphorylase converts α‐ d ‐glucose 1‐fluoride and phosphate into α‐ d ‐glucose 1‐phosphate, a reaction requiring the stereospecific protonation of the glucosyl fluoride by a Brønsted acid. The results are discussed with regard to a plausible reaction mechanism of fungal trehalose phosphorylase.