Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824

M. Tangney; G. T. Winters; W. J. Mitchell

doi:10.1038/sj.jim.7000125

Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824

M. Tangney, G. T. Winters, W. J. Mitchell

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	298-306
Number of pages	9
Journal	Journal of Industrial Microbiology and Biotechnology
Volume	27
Issue number	5
DOIs	https://doi.org/10.1038/sj.jim.7000125
Publication status	Published - 2001

Keywords

MalPH
Maltose 6-phosphate hydrolase
Phosphotransferase system

Access to Document

10.1038/sj.jim.7000125

Cite this

@article{efdc2f584f454a7880041216f50bd40d,

title = "Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824",

abstract = "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.",

keywords = "MalPH, Maltose 6-phosphate hydrolase, Phosphotransferase system",

author = "M. Tangney and Winters, \{G. T.\} and Mitchell, \{W. J.\}",

year = "2001",

doi = "10.1038/sj.jim.7000125",

language = "English",

volume = "27",

pages = "298--306",

journal = "Journal of Industrial Microbiology and Biotechnology",

issn = "1367-5435",

publisher = "Oxford University Press",

number = "5",

}

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 - https://www.scopus.com/pages/publications/0035674776

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 -

Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this