Maize recombinant C-4-pyruvate,orthophosphate dikinase: Expression in Escherichia coli, partial purification, and characterization of the phosphorylatable protein

被引：8

作者：

Chastain, CJ ^{[1
]}

Thompson, BJ ^{[1
]}

Chollet, R ^{[1
]}

机构：

[1] UNIV NEBRASKA, DEPT BIOCHEM, GW BEADLE CTR, LINCOLN, NE 68588 USA

来源：

PHOTOSYNTHESIS RESEARCH | 1996年 / 49卷 / 01期

关键词：

C-4; photosynthesis; plant; maize (Zea mays); PPDK; pyruvate; orthophosphate dikinase; recombinant enzyme;

D O I：

10.1007/BF00029430

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

The gene for C-4-pyruvate,orthophosphate dikinase (PPDK) from maize (Zea mays) was cloned into an Escherichia coli expression vector and recombinant PPDK produced in E. coli cells. Recombinant enzyme was found to be expressed in high amounts (5.3 U purified enzyme-activity liter(-1) of induced cells) as a predominantly soluble and active protein. Biochemical analysis of partially purified recombinant PPDK showed this enzyme to be equivalent to enzyme extracted from illuminated maize leaves with respect to (i) molecular mass, (ii) specific activity, (iii) substrate requirements, and (iv) phosphorylation/inactivation by its bifunctional regulatory protein.

引用

页码：83 / 89

页数：7

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