Characterization and regulation of phosphatidylglycerolphosphate phosphatase in Saccharomyces cerevisiae

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

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cobalt / pharmacology
  • Enzyme Stability
  • Glucose / pharmacology
  • Glycerol / pharmacology
  • Hydrogen-Ion Concentration
  • Inositol / pharmacology
  • Magnesium / pharmacology
  • Mitochondria / enzymology
  • Octoxynol
  • Phospholipids / metabolism
  • Phospholipids / pharmacology
  • Phosphoric Monoester Hydrolases / metabolism*
  • Polyethylene Glycols / pharmacology
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / ultrastructure
  • Substrate Specificity
  • Temperature

Substances

  • Phospholipids
  • Cobalt
  • Polyethylene Glycols
  • Inositol
  • Octoxynol
  • Phosphoric Monoester Hydrolases
  • phosphatidylglycerophosphatase
  • Magnesium
  • Glucose
  • Glycerol