Acetate catabolism in the dissimilatory iron-reducing isolate GS-15

J Bacteriol. 1991 Apr;173(8):2704-6. doi: 10.1128/jb.173.8.2704-2706.1991.

Abstract

Acetate-grown GS-15 whole-cell suspensions were disrupted with detergent and assayed for enzymes associated with acetate catabolism. Carbon monoxide dehydrogenase and formate dehydrogenase were not observed in GS-15. Catabolic levels of acetokinase and phosphotransacetylase were observed. Enzyme activities of the citric acid cycle, i.e., isocitrate dehydrogenase, 2-oxoglutarate sythase, succinate dehydrogenase, fumarase, and malate dehydrogenase, were observed.

Publication types

  • Comparative Study

MeSH terms

  • Acetate Kinase / analysis
  • Acetates / metabolism*
  • Acetyl Coenzyme A / metabolism*
  • Bacteria / metabolism*
  • Carbon Monoxide / metabolism
  • Citric Acid Cycle
  • Electron Transport
  • Euryarchaeota / enzymology
  • Euryarchaeota / metabolism
  • Fumarate Hydratase
  • Isocitrate Dehydrogenase / analysis
  • Ketone Oxidoreductases / analysis
  • Malate Dehydrogenase / analysis
  • Phosphate Acetyltransferase / analysis
  • Pseudomonas aeruginosa / enzymology
  • Pseudomonas aeruginosa / metabolism
  • Succinate Dehydrogenase / analysis

Substances

  • Acetates
  • Acetyl Coenzyme A
  • Carbon Monoxide
  • Malate Dehydrogenase
  • Isocitrate Dehydrogenase
  • Ketone Oxidoreductases
  • 2-oxoglutarate synthase
  • Succinate Dehydrogenase
  • Phosphate Acetyltransferase
  • Acetate Kinase
  • Fumarate Hydratase