1981
DOI: 10.2323/jgam.27.239
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Mode of action of a bacteriocin from Erwinia carotovora III. properties of phospholipase a of erwinia carotovora and its involvement in phospholipid degradation caused by carotovoricin.

Abstract: Phospholipase A in the outer membrane of Erwinia carotovora 645ArT was found to be activated by various detergents such as cholate, deoxycholate and Triton X-100, and methanol. The enzyme was inhibited by ethylenediaminetetraacetic acid, and Ca2+ was required for the enzyme activity. The enzyme hydrolyzed phosphatidylethanolamine and phosphatidylglycerol to form nearly equimolar amounts of free fatty acids and lysophospholipids. Cardiolipin, however, was not susceptible to the enzyme. In a mutant strain defici… Show more

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Cited by 5 publications
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“…Extracellular enzymes produced by E. carotovora subsp. carotovora capable of degrading plant cell wall and plant cell membrane components include the following: endo-pectate lyase, endo-polygalacturonase, cellulase, protease, phosphatidase C, and phosholipase A (2,8,9,18,20,22). In an effort to clarify the role of Erwinia pectic enzymes in pathogenesis, several laboratories have isolated genes encoding enzymatic pathogenic determinants from Erwinia spp.…”
mentioning
confidence: 99%
“…Extracellular enzymes produced by E. carotovora subsp. carotovora capable of degrading plant cell wall and plant cell membrane components include the following: endo-pectate lyase, endo-polygalacturonase, cellulase, protease, phosphatidase C, and phosholipase A (2,8,9,18,20,22). In an effort to clarify the role of Erwinia pectic enzymes in pathogenesis, several laboratories have isolated genes encoding enzymatic pathogenic determinants from Erwinia spp.…”
mentioning
confidence: 99%