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Separation of Four Components of the Phosphoenolpyruvate: Glucose Phosphotransferase System in Vibrio parahaemolyticus
Author(s) -
Kubota Yoneo,
Iuchi Shiro,
Fujisawa Asako,
Tanaka Shuji
Publication year - 1979
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1979.tb00450.x
Subject(s) - vibrio parahaemolyticus , biology , phosphoenolpyruvate carboxykinase , pep group translocation , vibrionaceae , microbiology and biotechnology , vibrio , biochemistry , bacteria , enzyme , genetics , gene
Four classes of Vibrio parahaemolyticus mutants defective in the phosphoenolpyruvate: glucose phosphotransferase system (PTS) are described. They were phenotypically different, and were defective in different PTS components. The components designated tentatively as II, I, III, and H were separated by gel filtration of a wild‐type extract. Component II, which was specific for glucose and found in the particulate fraction, is probably membrane‐bound, glucose‐specific enzyme II. Both components I and H were soluble proteins, and the latter was relatively heat‐stable. Component I was required for phosphorylation of glucose, trehalose, fructose, mannose, and mannitol. Component H was also required for phosphorylating all the above sugars except fructose. These and some additional findings strongly suggest that components I and H correspond to enzyme I and HPr, respectively. Component III, a soluble heat‐stable protein, may be equivalent to the sugar‐specific factor III found in other organisms, although it seems to participate in phosphorylating two sugars, glucose and trehalose. There were evidences that mutants defective in components I and III were deficient in cyclic adenosine 3′,5′‐monophosphate synthesis under certain conditions.