ESSENTIAL ARGINYL RESIDUE IN YEAST HEXOKINASE

被引：44

作者：

PHILIPS, M ^{[1
]}

PHO, DB ^{[1
]}

PRADEL, LA ^{[1
]}

机构：

[1] COLL FRANCE, BIOCHIM CELLULAIRE LAB, F-75005 PARIS, FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 566卷 / 02期

关键词：

(Yeast); Arginyl residue; Hexokinase;

D O I：

10.1016/0005-2744(79)90033-0

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：

The inactivation of yeast hexokinase A (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) by phenylglyoxal obeys pseudo 1st-order kinetics. Formation of a reversible enzyme-reagent complex prior to modification is suggested by the observed saturation kinetics. Loss of activity correlates with the incorporation of 1 mol of [14C]phenylglyoxal/mol 50,000 dalton subunit. No significant conformational change occurs concomitantly. Inactivation is attributable to modification of an arginyl residue. The pattern of protection by substrates and analogs favors an interaction of this essential resude with the terminal phosphoryl group of ATP or G-6-P.

引用

页码：296 / 304

页数：9

共 32 条

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