Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824
Autor: | GT Winters, WJ Mitchell, M Tangney |
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Rok vydání: | 2000 |
Předmět: |
Sucrose
Clostridium acetobutylicum Molecular Sequence Data Bioengineering Biology Cell Fractionation Applied Microbiology and Biotechnology Microbiology chemistry.chemical_compound Bacterial Proteins Hydrolase Amino Acid Sequence Phosphorylation Maltose Phosphoenolpyruvate Sugar Phosphotransferase System Maltose transport chemistry.chemical_classification Clostridium Base Sequence Cell-Free System Sequence Homology Amino Acid Biological Transport alpha-Glucosidases PEP group translocation Industrial microbiology biology.organism_classification Enzyme Glucose Biochemistry chemistry Genes Bacterial Phosphoenolpyruvate carboxykinase Biotechnology |
Zdroj: | Journal of industrial microbiologybiotechnology. 27(5) |
ISSN: | 1367-5435 |
Popis: | The utilization of maltose by Clostridium acetobutylicum ATCC 824 was investigated. Glucose was used preferentially to maltose, when both substrates were present in the medium. Maltose phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) activity was detected in extracts prepared from cultures grown on maltose, but not glucose or sucrose, as the sole carbon source. Extract fractionation and PTS reconstitution experiments revealed that the specificity for maltose is contained entirely within the membrane in this organism. A putative gene system for the maltose PTS was identified (from the C. acetobutylicum ATCC 824 genome sequence), encoding an enzyme IIMal and a maltose 6-phosphate hydrolase. Journal of Industrial Microbiology & Biotechnology (2001) 27, 298–306. |
Databáze: | OpenAIRE |
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