The location of the arginine-specific carboxypeptidase in the membrane of Mycoplasma salivarium and its physiological functions.
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.
Shibata
K
K
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
Watanabe
T
T
D001120:Arginine / Q000378:metabolism; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002268:Carboxypeptidases / Q000302:isolation & purification* / Q000502:physiology; D002455:Cell Division; D002462:Cell Membrane / Q000201:enzymology; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000502:physiology; D009174:Mycoplasma / Q000201:enzymology* / Q000254:growth & development; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008565:Membrane Proteins; D001120:Arginine; D002268:Carboxypeptidases