Reaction pathway of tryptophanase degrading D-tryptophan

被引：4

作者：

Shimada, A ^{[1
]}

Kogure, H ^{[1
]}

Shishido, H ^{[1
]}

Nakamura, I ^{[1
]}

机构：

[1] SAGAMI WOMENS UNIV,DEPT FOOD & NUTR,SAGAMIHARA,KANAGAWA,JAPAN

来源：

AMINO ACIDS | 1997年 / 12卷 / 3-4期

关键词：

amino acids; tryptophanase; D-tryptophan; diammonium-hydrogen phosphate; kinetic analysis; stereospecificity;

D O I：

10.1007/BF01373018

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：

Tryptophanase, which has the very strict stereospecificity to L-tryptophan under ordinary condition, becomes active to D-tryptophan in highly concentrated diammoniumhydrogen phosphate solution. The reaction process of D-tryptophan degradation is studied in terms of kinetics. Diammoniumhydrogen phosphate acts on tryptophanase as activator below 3.1 M, and as noncompetitive inhibitor over it. Additionally, the pathway of the reaction is provided on the basis of kinetic parameters.

引用

页码：379 / 383

页数：5

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