[Regulation of PEP-carboxylase of the facultative methylotrop Acetobacter sp. MB 58]

Z Allg Mikrobiol. 1982;22(7):453-63. doi: 10.1002/jobm.3630220705.
[Article in German]

Abstract

Acetobacter sp. MB 58 assimilates methanol via the fructose-1,6-bisphosphate variant of the hexulose phosphate pathway. Glyceraldehyde-3-phosphate originates as net product of an assimilation loop involving the regeneration of the C1-acceptor ribulose-5-phosphate and must be available for the de novo synthesis of the C1-acceptor as well as for the oxidative glycolysis. It is made probable in a regulatory model that this is accomplished via alternating anabolic and catabolic phases which are controlled by concerted action of PEP-carboxylase and pyruvate kinase. Whereas Ac-CoA is a crucial effector and alpha-ketoglutarate and aspartate are inhibitors for the PEP-carboxylase, the pyruvate kinase is assumed to be regulated by energy charge.

MeSH terms

  • Acetobacter / enzymology*
  • Acetyl Coenzyme A / metabolism
  • Adenine Nucleotides / pharmacology
  • Aspartic Acid / pharmacology
  • Carboxy-Lyases / metabolism*
  • Hydrogen-Ion Concentration
  • Ketoglutaric Acids / pharmacology
  • Magnesium / pharmacology
  • Methanol / metabolism*
  • Models, Biological
  • Phosphoenolpyruvate Carboxylase / metabolism*
  • Pyruvate Kinase / metabolism

Substances

  • Adenine Nucleotides
  • Ketoglutaric Acids
  • Aspartic Acid
  • Acetyl Coenzyme A
  • Pyruvate Kinase
  • Carboxy-Lyases
  • Phosphoenolpyruvate Carboxylase
  • Magnesium
  • Methanol