This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Thompson, J Articles by Robrish, S A Search for Related Content PubMed PubMed Citation Articles by Thompson, J Articles by Robrish, S A

research-article

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

Laboratory of Microbial Ecology, National Institute of Dental Research, Bethesda, Maryland.

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.

This article has been cited by other articles:

• Caescu, C. I., Vidal, O., Krzewinski, F., Artenie, V., Bouquelet, S. (2004). Bifidobacterium longum Requires a Fructokinase (Frk; ATP:D-Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism. J. Bacteriol. 186: 6515-6525 [Abstract] [Full Text]  
• Pikis, A., Immel, S., Robrish, S. A., Thompson, J. (2002). Metabolism of sucrose and its five isomers by Fusobacterium mortiferum. Microbiology 148: 843-852 [Abstract] [Full Text]