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The Substrate Spectrum of Mandelate Racemase: Minimum Structural Requirements for Substrates and Substrate Model
Author(s) -
Felfer Ulfried,
Goriup Marian,
Koegl Marion F.,
Wagner Ulrike,
LarisseggerSchnell Barbara,
Faber Kurt,
Kroutil Wolfgang
Publication year - 2005
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200505012
Subject(s) - racemization , substrate (aquarium) , chemistry , kinetic resolution , cofactor , stereochemistry , substrate specificity , enzyme , combinatorial chemistry , enantioselective synthesis , catalysis , organic chemistry , oceanography , geology
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 summarizes all aspects of mandelate racemase relevant for the application of this enzyme in preparative‐scale biotransformations with special emphasis on its substrate tolerance. Collection and evaluation of substrate structure‐activity data led to a set of general guidelines, which were used as basis for the construction of a general substrate model, which allows a quick estimation of the expected activity for a given substrate.