TY - JOUR
T1 - Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824
AU - Tangney, M.
AU - Winters, G. T.
AU - Mitchell, W. J.
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
KW - MalPH
KW - Maltose 6-phosphate hydrolase
KW - Phosphotransferase system
UR - http://www.scopus.com/inward/record.url?scp=0035674776&partnerID=8YFLogxK
U2 - 10.1038/sj.jim.7000125
DO - 10.1038/sj.jim.7000125
M3 - Article
SN - 1367-5435
VL - 27
SP - 298
EP - 306
JO - Journal of Industrial Microbiology and Biotechnology
JF - Journal of Industrial Microbiology and Biotechnology
IS - 5
ER -