Open AccessAn Escherichia coli mutant deficient in pyruvate oxidase activity due to altered phospholipid activation of the enzyme
Author(s) -
Yingying Chang,
John E. Cronan
Publication year - 1984
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.81.14.4348
Subject(s) - escherichia coli , mutant , biochemistry , enzyme , oxidase test , oxidoreductase , enzyme activator , chemistry , biology , gene
The pyruvate oxidase (pyruvate:ferricytochromeb 1 oxidoreductase, EC 1.2.2.2) ofEscherichia coli is markedly activated by phospholipidsin vitro . To test the physiological relevance of this activation, we isolated anE. 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 poorlyin vivo , indicating that activation of the oxidase by phospholipids plays an important physiological role.