Determination of the time course of an enzymatic reaction by H-1 NMR spectroscopy: Hydroxynitrile lyase catalysed transhydrocyanation

被引：12

作者：

Hickel, A

Gradnig, G

Griengl, H

Schall, M

Sterk, H

机构：

[1] KARL FRANZENS UNIV GRAZ,INST BIOCHEM,A-8010 GRAZ,AUSTRIA

[2] KARL FRANZENS UNIV GRAZ,INST ORGAN CHEM,A-8010 GRAZ,AUSTRIA

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 1996年 / 52卷 / 01期

关键词：

aqueous system; hydroxynitrile lyase; H-1 NMR spectroscopy; transhydrocyanation;

D O I：

10.1016/0584-8539(95)01574-4

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

The time course of the enzyme catalysed transhydrocyanation of benzaldehyde to give (S)-mandelonitrile was investigated using a hydroxynitrile lyase from Hevea brasiliensis as catalyst and acetone cyanohydrin as cyanide donor. Employing special techniques it was possible to apply H-1 NMR spectroscopy in aqueous medium to monitor the concentration changes of all substrates and products. By this technique strong evidence for inhibition of the enzyme at higher substrate concentrations was obtained.

引用

页码：93 / 96

页数：4

共 20 条

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[2]

BERETON IM, 1989, J MAG RESON, V81, P411

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