The substrate spectrum of mandelate racemase: minimum structural requirements for substrates and substrate model

…, U Wagner, B Larissegger??Schnell…

文献索引：Felfer, Ulfried; Goriup, Marian; Koegl, Marion F.; Wagner, Ulrike; Larissegger-Schnell, Barbara; Faber, Kurt; Kroutil, Wolfgang Advanced Synthesis and Catalysis, 2005 , vol. 347, # 7-8 p. 951 - 961

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被引用次数: 32

摘要

Abstract Mandelate racemase (EC 5.1. 2.2) is one of the few biochemically well- characterized racemases. The remarkable stability of this cofactor-independent enzyme and its broad substrate tolerance make it an ideal candidate for the racemization of non-natural α- hydroxycarboxylic acids under physiological reaction conditions to be applied in deracemization protocols in connection with a kinetic resolution step. This review ...