INITIAL CHARACTERIZATION OF SUCROSE-6-PHOSPHATE HYDROLASE FROM STREPTOCOCCUS-MUTANS AND ITS APPARENT IDENTITY WITH INTRACELLULAR INVERTASE

被引:37
作者
CHASSY, BM
PORTER, EV
机构
[1] Microbiology Section, Laboratory of Microbiology and Immunology NIDR, NIH, Bethesda
关键词
D O I
10.1016/0006-291X(79)90979-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
An intracellular enzyme catalyzing the hydrolysis of sucrose-6-phosphate to glucose-6-phosphate and fructose has been identified in extracts of Streptococcus mutans 6715-10. The preparation was purified chromatographically and found to have an apparent molecular weight of 42,000. The enzyme has as a Km for sucrose-6-phosphate of 0.21 mM, a pH optimum of 7.1, is quite stable and requires no added cofactors or metal ions. Sucrose is a competitive inhibitor of sucrose-6-phosphate hydrolysis (Ki = 8. 12 mM). A previously described intracellular invertase copurifies with the enzyme and could not be separated from it by disc gel electrophoresis. It is concluded that intracellular invertase is a sucrose-6-phosphate hydrolase with a low catalytic activity for hydrolysis of sucrose. © 1979.
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页码:307 / 314
页数:8
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