Open AccessThe location of the arginine‐specific carboxypeptidase in the membrane of Mycoplasma salivarium and its physiological functions
Author(s) -
Shibata Kenichiro,
Watanabe Tsuguo
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05293.x
Subject(s) - arginine , carboxypeptidase , biochemistry , membrane , enzyme , chemistry , mycoplasma , growth medium , microbiology and biotechnology , biology , bacteria , amino acid , genetics
A non‐penetrating probe, 2,4,6‐trinitrobenzenesulfonate, inhibited the activity of the carboxypeptidase purified from the cell membranes of Mycoplasma salivarium and the same enzymatic activity of intact Mycoplasma cells as well. Growth of the organism in medium containing benzoylglycyl‐ l ‐arginine resulted in a higher pH and higher turbidity than growth in the same medium without this supplement. It was concluded that the enzyme existed in the outer surface of the membrane of the cells and probably functioned to supply the organism with arginine as an energy source.