Escherichia coli molybdoenzymes can be activated by protein FA from several gram-negative bacteria

J Gen Microbiol. 1989 Dec;135(12):3467-75. doi: 10.1099/00221287-135-12-3467.

Abstract

Six Gram-negative bacteria (Klebsiella pneumoniae, Erwinia chrysanthemi, Proteus vulgaris, Serratia marescens, Salmonella typhimurium, and Pseudomonas aeruginosa) were shown to contain an FA-type protein capable of activating aponitrate reductase, apotrimethylamine N-oxide reductase and apoformate dehydrogenase of Escherichia coli. Protein FA activity was highest in Erwinia chrysanthemi and lowest in Pseudomonas aeruginosa. All the species also contained the low-Mr (less than or equal to 1500) heat-resistant material previously reported to be necessary for the protein-FA-dependent activation of E. coli chlB nitrate reductase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Coenzymes / metabolism
  • Enterobacteriaceae / enzymology
  • Enzyme Activation
  • Escherichia coli / enzymology*
  • Formate Dehydrogenases / metabolism
  • Metalloproteins / metabolism
  • Molybdenum
  • Molybdenum Cofactors
  • NADH, NADPH Oxidoreductases / metabolism
  • Nitrate Reductase
  • Nitrate Reductases / metabolism*
  • Oxidoreductases Acting on CH-NH Group Donors
  • Pteridines / metabolism

Substances

  • Bacterial Proteins
  • Coenzymes
  • Metalloproteins
  • Molybdenum Cofactors
  • Pteridines
  • Molybdenum
  • molybdenum cofactor
  • Formate Dehydrogenases
  • methylamine dehydrogenase
  • Oxidoreductases Acting on CH-NH Group Donors
  • NADH, NADPH Oxidoreductases
  • Nitrate Reductases
  • Nitrate Reductase