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Biochim Biophys Acta. 1990 Sep 18;1046(2):144-50.

Characterization and regulation of phosphatidylglycerolphosphate phosphatase in Saccharomyces cerevisiae.

Author information

1
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606.

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.

PMID:
2171664
DOI:
10.1016/0005-2760(90)90181-v
[Indexed for MEDLINE]
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