Department of Microbiology, University of Illinois, 131 Burrill Hall, 407 South Goodwin, Urbana, IL 61801.
Proc Natl Acad Sci U S A. 1984 Jul;81(14):4348-52. doi: 10.1073/pnas.81.14.4348.
The pyruvate oxidase (pyruvate:ferricytochrome b(1) oxidoreductase, EC 1.2.2.2) of Escherichia coli is markedly activated by phospholipids in vitro. To test the physiological relevance of this activation, we isolated an E. coli mutant producing an oxidase that is deficient in activation by (and binding to) phospholipids. The mutant oxidase could be fully activated by a specific proteolytic cleavage, indicating that the catalytic site is normal. The mutant enzyme functions poorly in vivo, indicating that activation of the oxidase by phospholipids plays an important physiological role.
大肠杆菌的丙酮酸氧化酶（丙酮酸：细胞色素 b(1)氧化还原酶，EC 1.2.2.2）在体外明显被磷脂激活。为了检验这种激活的生理相关性，我们分离出一株产氧化酶的大肠杆菌突变株，该酶对磷脂的激活（和结合）缺陷。突变的氧化酶可以被一种特定的蛋白水解切割完全激活，表明催化部位正常。突变酶在体内功能不良，表明磷脂对氧化酶的激活在生理上起着重要作用。
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