Inactivation of human liver arginase by Woodward's reagent K:: Evidence for reaction with His141

被引：6

作者：

Carvajal, N ^{[1
]}

Uribe, E ^{[1
]}

López, V ^{[1
]}

Salas, M ^{[1
]}

机构：

[1] Univ Concepcion, Dept Biol Mol, Fac Ciencias Biol, Concepcion, Chile

来源：

PROTEIN JOURNAL | 2004年 / 23卷 / 03期

关键词：

arginase; human liver; histidine residue; site-directed mutagenesis; Woodward's reagent K;

D O I：

10.1023/B:JOPC.0000026413.68088.e0

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：

Human liver arginase (EC 3.5.3.1) was totally inactivated by incubation with Woodward's reagent K (WRK). The inactivation followed pseudo-first-order kinetics, and the order of the inactivation was close to 1, consistent with reaction of one molecule of WRK with one subunit molecule for inactivation. The effect was totally reversed by 0.5 M hydroxylamine, and reactivated species were inactivated again by a second incubation with WRK. The pH dependence of the pseudo-first-order rate constants of inactivation indicated the participation of a ionizable residue with a pK(a) of 6.3 at 25degreesC. Replacement of His 141 with phenylalanine rendered the enzyme totally resistant to the inactivation. We conclude that His 141 is the residue whose chemical modification with WRK inactivates the enzyme.

引用

页码：179 / 183

页数：5

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