An Escherichia coli mutant deficient in pyruvate oxidase activity due to altered phospholipid activation of the enzyme

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Abstract
The pyruvate oxidase (pyruvate:ferricytochrome b1 oxidoreductase, EC 1.2.2.2) of E. coli is markedly activated by phospholipids in vitro. To test the physiological relevance of this activation, an E. coli mutant producing an oxidase that is deficient in activation by (and binding to) phospholipids was isolated. The mutant oxidase could be fully activated by a specific proteolytic cleavage, indicatng that the catalytic site is normal. The mutant enzyme functioned poorly in vivo, indicating that activation of the oxidase by phospholipids plays an important physiological role.