INACTIVATION OF HISTIDINE AMMONIA-LYASE FROM STREPTOMYCES-GRISEUS BY DICARBONYL REAGENTS

被引：1
|
作者：
WHITE, PJ
KENDRICK, KE
机构：
[1] Department of Microbiology, Ohio State University, Columbus, OH
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1163卷 / 03期
关键词：
DICARBONYL; HISTIDASE; HUT GENE; METHYLGLYOXAL; PHENYLGLYOXAL; (S-GRISEUS);
D O I：
10.1016/0167-4838(93)90162-K
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：
Histidine ammonia-lyase from Streptomyces griseus was inactivated by methylglyoxal and phenylglyoxal, dicarbonyl reagents known to react specifically with arginyl residues in proteins. The inactivation showed pseudo-first-order kinetics and could be prevented by protection with histidinol phosphate, a competitive inhibitor of histidine ammonia-lyase. Analysis of the amino acid composition of histidine ammonia-lyase after treatment with phenylglyoxal, together with the kinetics of inactivation, suggested that inactivation was a consequence of specific reaction with one or more essential arginyl residues at or near the active site of the enzyme.
引用
收藏
页码：273 / 279
页数：7
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