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. 1984 Dec;160(3):1031–1036. doi: 10.1128/jb.160.3.1031-1036.1984

gamma-Glutamyltranspeptidase from Proteus mirabilis: localization and activation by phospholipids.

R Nakayama, H Kumagai, T Tochikura
PMCID: PMC215814  PMID: 6150026

Abstract

Antiserum was prepared against the purified gamma-glutamyltranspeptidase (EC 2.3.2.2) of Proteus mirabilis. The antiserum inactivated the gamma-glutamyltranspeptidase activities of both purified enzyme and intact cells. Native cells were agglutinated with the antibody. Immunocytochemical studies with indirect immunofluorescence and electron microscopy analysis suggested that gamma-glutamyltranspeptidase is localized on the surface of the cell. Its distribution in the cell wall or periplasmic space or both was also confirmed by the treatment of cells with lysozyme-EDTA. The purified enzyme was activated by the addition of membrane phospholipids isolated from the same bacterium. The hydrolysis activity was stimulated more than the transpeptidation activity by several phospholipids.

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