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. 1990 Sep 18;1046(2):144-50.
doi: 10.1016/0005-2760(90)90181-v.

Characterization and regulation of phosphatidylglycerolphosphate phosphatase in Saccharomyces cerevisiae

B L Kelly  1 , M L Greenberg
Affiliations
Free article

Characterization and regulation of phosphatidylglycerolphosphate phosphatase in Saccharomyces cerevisiae

B L Kelly et al. Biochim Biophys Acta. .
Free article

Abstract

Phosphatidylglycerophosphatase (EC 3.1.3.27) activity was characterized in mitochondrial extracts from Saccharomyces cerevisiae. The enzyme has a pH optimum of 5.5. Maximum activity occurs in the presence of Triton X-100 (5 mM) and cobalt or magnesium ions (5 mM). The apparent Km for PGP is 14.6 microM. The temperature optimum is between 50 degrees C and 60 degrees C. The enzyme is labile above 50 degrees C. The presence of inositol in growth media results in a slight but reproducible increase in PGPase activity in mitochondrial extracts from glucose-grown cells but not glycerol-grown cells. The inositol effect is not seen in crude cell extracts. Carbon source does not affect PGPase activity in mitochondrial extracts or in crude cell extracts.

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