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. 1979 Nov;26(2):487–491. doi: 10.1128/iai.26.2.487-491.1979

Regulation and function of sucrose 6-phosphate hydrolase in Streptococcus mutans.

E J St Martin, C L Wittenberger
PMCID: PMC414642  PMID: 94907

Abstract

Sucrose catabolism by Streptococcus mutans is initiated by a phosphoenolpyruvate-dependent sucrose phosphotransferase reaction that produces sucrose 6-phosphate the latter is then cleaved by a sucrose 6-phosphate hydrolase reaction that yields glucose 6-phosphate and fructose. We have examined the regulation of the sucrose 6-phosphate hydrolase and found that it was synthesized constitutively whereas sucrose phosphotransferase activity was inducible. However, the levels of both sucrose phosphotransferase and sucrose 6-phosphate hydrolase were repressed when fructose was used as a growth substrate. The specific activity of sucrose 6-phosphate hydrolase in permeabilized cells was approximately 30 mmol/min per mg (dry weight of cells), and it had an apparent Km for sucrose 6-phosphate of 0.3 mM. analysis of a mutant that was missing sucrose 6-phosphate hydrolase activity revealed that its ability to hydrolyze sucrose was reduced.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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