Fructose-1,6-bisphosphate aldolase from Vibrio marinus, a psychrophilic marine bacterium

Z Allg Mikrobiol. 1979;19(2):97-106. doi: 10.1002/jobm.3630190205.

Abstract

Fructose-1,6-bisphosphate aldolase (Fru-P2A) from a psychrophilic marine bacterium was found to be Class II aldolase based on activation by K+, activation by divalent cations, inactivation by EDTA, low molecular weight, and similar values for Km, Vmax, and Arrhenius activation energy. This enzyme was not markedly different in amino acid composition from the enzymes from mesophilic and thermophilic organisms, yet it has unusual thermal properties.

MeSH terms

  • Amino Acids / analysis
  • Cold Temperature
  • Edetic Acid / pharmacology
  • Enzyme Activation
  • Fructose-Bisphosphate Aldolase / metabolism*
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Potassium / pharmacology
  • Seawater
  • Vibrio / enzymology*
  • Water Microbiology

Substances

  • Amino Acids
  • Edetic Acid
  • Fructose-Bisphosphate Aldolase
  • Potassium