Substrate spectrum of mandelate racemase -: Part 1:: Variation of the α-hydroxy acid moiety

被引：13

作者：

Goriup, M ^{[1
]}

Strauss, UT ^{[1
]}

Felfer, U ^{[1
]}

Kroutil, W ^{[1
]}

Faber, K ^{[1
]}

机构：

[1] Dept Chem Organ & Bioorgan Chem, A-8010 Graz, Austria

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2001年 / 15卷 / 4-6期

基金：

奥地利科学基金会;

关键词：

mandelate racemase; racemization; mandelic acid amide; Pseudomonas putida ATCC 12633; p-Bromo mandelic acid amide;

D O I：

10.1016/S1381-1177(01)00036-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Enzymatic racemization of mandelic acid derivatives modified at the a-hydroxy acid moiety was achieved using mandelate racemase [EC 5.1.2.2]. Whereas a-amino acid derivatives, such as phenyl glycine and mandelic acid hydrazide were not accepted, the mandelic acid amide was racemized at an acceptable rate. The latter was significantly enhanced by an electron-withdrawing substituent in the phenyl moiety. Based on the catalytic mechanism of the enzyme, the relative activities of non-natural substrates could be explained by steric and electronic reasons. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：207 / 212

页数：6

共 29 条

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