The pyruvate oxidase (pyruvate:ferricytochrome b1 oxidoreductase, EC 220.127.116.11) 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.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Issue number||14 I|
|State||Published - 1984|
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