Sucrose fermentation by Fusobacterium mortiferum ATCC 25557: transport, catabolism, and products

J Bacteriol. 1992 May;174(10):3227-35. doi: 10.1128/jb.174.10.3227-3235.1992.

Abstract

Studies of sucrose utilization by Fusobacterium mortiferum ATCC 25557 have provided the first definitive evidence for phosphoenolpyruvate-dependent sugar:phosphotransferase activity in the family Bacteroidaceae. The phosphoenolpyruvate-dependent sucrose:phosphotransferase system and the two enzymes required for the dissimilation of sucrose 6-phosphate are induced specifically by growth of F. mortiferum on the disaccharide. Monomeric sucrose 6-phosphate hydrolase (M(r), 52,000) and a dimeric ATP-dependent fructokinase (subunit M(r), 32,000) have been purified to electrophoretic homogeneity. The physicochemical and catalytic properties of these enzymes have been examined, and the N-terminal amino acid sequences for both proteins are reported. The characteristics of sucrose 6-phosphate hydrolase and fructokinase from F. mortiferum are compared with the same enzymes from both gram-positive and gram-negative species. Butyric, acetic, and D-lactic acids are the end products of sucrose fermentation by F. mortiferum. A pathway is proposed for the translocation, phosphorylation, and metabolism of sucrose by this anaerobic pathogen.

MeSH terms

  • Acetates / metabolism
  • Acetic Acid
  • Amino Acid Sequence
  • Biological Transport, Active
  • Butyrates / metabolism
  • Enzyme Induction
  • Fusobacterium / metabolism*
  • Glycoside Hydrolases / isolation & purification
  • Glycoside Hydrolases / metabolism
  • Lactates / metabolism
  • Lactic Acid
  • Molecular Sequence Data
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Phosphofructokinase-1 / isolation & purification
  • Phosphofructokinase-1 / metabolism
  • Substrate Specificity
  • Sucrose / metabolism*
  • beta-Fructofuranosidase

Substances

  • Acetates
  • Butyrates
  • Lactates
  • Lactic Acid
  • Sucrose
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • Phosphofructokinase-1
  • Glycoside Hydrolases
  • beta-Fructofuranosidase
  • Acetic Acid