Physiological functions of NAD- and NADP-linked malic enzymes in Escherichia coli

Biochem Biophys Res Commun. 1971 May 21;43(4):875-81. doi: 10.1016/0006-291x(71)90698-x.
No abstract available

MeSH terms

  • Acetates / pharmacology
  • Aspartic Acid / pharmacology
  • Binding Sites
  • Carbon Isotopes
  • Cell-Free System
  • Centrifugation
  • Coenzyme A / metabolism
  • Culture Media
  • Depression, Chemical
  • Enzyme Induction
  • Enzyme Repression
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Escherichia coli / growth & development
  • Fatty Acids / biosynthesis
  • Glucose / antagonists & inhibitors
  • Glucose / pharmacology
  • Glutamates / pharmacology
  • Glycerol / pharmacology
  • Glycolysis
  • Lactates / pharmacology
  • Malate Dehydrogenase / biosynthesis*
  • Malate Dehydrogenase / physiology
  • Malates / metabolism
  • Malates / pharmacology
  • Models, Biological
  • Models, Chemical
  • NAD*
  • NADP*
  • Pyruvates / metabolism
  • Spectrophotometry
  • Stimulation, Chemical
  • Succinates / metabolism
  • Succinates / pharmacology
  • Vibration

Substances

  • Acetates
  • Carbon Isotopes
  • Culture Media
  • Fatty Acids
  • Glutamates
  • Lactates
  • Malates
  • Pyruvates
  • Succinates
  • NAD
  • Aspartic Acid
  • NADP
  • Malate Dehydrogenase
  • Glucose
  • Glycerol
  • Coenzyme A