Role of C-terminal domains in surface attachment of the fructosyltransferase of Streptococcus salivarius ATCC 25975

The cell-associated beta-D-fructosyltransferase of Streptococcus salivarius, which is devoid of the cell wall anchoring motif, LPXTG, is released on exposure to its substrate, sucrose. Deletions within the C terminus of the enzyme implicated both the hydrophobic and the proline-glycine-serine-threon...

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Veröffentlicht in:	Journal of bacteriology 1998-12, Vol.180 (23), p.6400-6403
Hauptverfasser:	Rathsam, C, Jacques, N A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacteriology Binding Sites - genetics Cell Membrane - drug effects Cell Membrane - enzymology Cells Enzyme Stability Enzymes Genetics and Molecular Biology Hexosyltransferases - chemistry Hexosyltransferases - genetics Hexosyltransferases - metabolism Mutagenesis, Site-Directed Protease Inhibitors - pharmacology Sequence Deletion Streptococcus - drug effects Streptococcus - enzymology Streptococcus - genetics Streptococcus salivarius
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Beschreibung
Zusammenfassung:	The cell-associated beta-D-fructosyltransferase of Streptococcus salivarius, which is devoid of the cell wall anchoring motif, LPXTG, is released on exposure to its substrate, sucrose. Deletions within the C terminus of the enzyme implicated both the hydrophobic and the proline-glycine-serine-threonine-rich wall-associated domain in stabilizing the enzyme on the cell surface.
ISSN:	0021-9193 1098-5530
DOI:	10.1128/JB.180.23.6400-6403.1998