Sucrose fermentation by Fusobacterium mortiferum ATCC 25557: transport, catabolism, and products
| Autor: | S A Robrish, N Y Nguyen, John F. Thompson |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Sucrose
Glycoside Hydrolases Phosphofructokinase-1 Molecular Sequence Data Disaccharide Biological Transport Active Acetates Biology Microbiology Fructokinase Substrate Specificity Phosphotransferase chemistry.chemical_compound Fusobacterium mortiferum Glycoside hydrolase Amino Acid Sequence Lactic Acid Phosphoenolpyruvate Sugar Phosphotransferase System Molecular Biology Acetic Acid beta-Fructofuranosidase PEP group translocation Fusobacterium Butyrates chemistry Biochemistry Enzyme Induction Lactates Fermentation Research Article |
| Zdroj: | Journal of Bacteriology. 174:3227-3235 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.174.10.3227-3235.1992 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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