| Autor: |
Felfer, Ulfried, Goriup, Marian, Koegl, Marion 4;F., Wagner, Ulrike, Larissegger-Schnell, Barbara, Faber, Kurt, Kroutil, Wolfgang |
| Zdroj: |
Advanced Synthesis & Catalysis; June 2005, Vol. 347 Issue: 7-8 p951-961, 11p |
| Abstrakt: |
Mandelate racemase (EC 4;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. |
| Databáze: |
Supplemental Index |
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