Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans.

Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Research Abstract Details 

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Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Abstract Text:

Ali O Kilic,Allen L Honeyman,Lin Tao,

Sugar metabolism by Streptococcus mutans is associated with tooth decay. The most abundant sugars in the human diet are sucrose and maltose, a derivative of starch. Previously, we reported a binding protein-dependent transport system (msm) in S. mutans that transports sucrose and maltose, but its associated enzymes do not metabolize maltose. By searching the S. mutans genomic sequence for a maltose system (mal), we found a gene cluster encoding proteins with homology to those of msm and the Escherichia coli maltose system. Mutants were constructed by deleting msm or mal, or both, and tested for sugar utilization. Deletion of the mal system diminished the ability of S. mutans to ferment maltose, but deletion of only the mal transporter genes or msm showed reduced utilization of chromogenic maltosides. Maltose, sucrose, glucose, fructose, mannose, and N-acetyl glucosamine inhibited utilization of chromogenic maltosides by the wild-type strain and mutants. In conclusion, the two binding protein-dependent systems in S. mutans appear to transport collaboratively their common substrate sugars, notably sucrose and maltose.

Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Publishing Authors By Initials

AO Kilic,AL Honeyman,L Tao,

For similar carbohydrates: polysaccharides: oligosaccharides: disaccharides: sucrose research abstracts see: carbohydrates: polysaccharides: oligosaccharides: disaccharides: sucrose research

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Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: FEMS microbiology letters

VOLUME: 266

Page Numbers: 218-23

Journal Abbreviation: FEMS Microbiol. Lett.

ISSN: 0378-1097

DAY: 3

MONTH: Jan

YEAR: 2007

Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7705721

Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Keywords Mesh Terms:

KEYWORDS: Sucrose

MESH TERMS: metabolism

Chemical & Substance for Abstract: Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans. Information

Substance Name: Maltose

Registry Number: 69-79-4

Grant and Affiliation Information for Overlapping substrate specificity for sucrose and maltose of two binding protein-dependent sugar uptake systems in Streptococcus mutans.

AFFILIATION: Department of Oral Biology, College of Dentistry, University of Illinois at Chicago, IL 60612, USA.

Country: England

AGENCY: United States NIDCR

GRANT: DE11400

ACRONYM: DE

MEDLINETA: FEMS Microbiol Lett

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