Regulation of phosphatidate phosphatase activity by inositol in Saccharomyces cerevisiae
نویسندگان
چکیده
منابع مشابه
Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases.
The regulation of Saccharomyces cerevisiae membrane-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) activity by sphingoid bases was examined using Triton X-100/lipid-mixed micelles. Sphingosine, phytosphingosine, and sphinganine inhibited purified preparations of the 104- and 45-kDa forms of phosphatidate phosphatase in a dose-dependent manner. The structu...
متن کاملPhosphorylase phosphatase activity in Saccharomyces cerevisiae 257.
A phosphatase, active towards phosphorylase a and phosphorylated proteins casein and histone II-A, was isolated from Saccharomyces cerevisiae 257. The enzyme dephosphorylated glycogen phosphorylase from commercial yeast rendering it inactive. The protein phosphatase activity was not influenced by any metal ions. Phosphorylase phosphatase activity was slightly stimulated by p-nitrophenyl phospha...
متن کاملPAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae.
In the yeast Saccharomyces cerevisiae, the synthesis of phospholipids in the exponential phase of growth occurs at the expense of the storage lipid triacylglycerol. As exponential phase cells progress into the stationary phase, the synthesis of triacylglycerol occurs at the expense of phospholipids. Early work indicates a role of the phosphatidate phosphatase (PAP) in this metabolism; the enzym...
متن کاملCharacterization and regulation of phosphatidylglycerolphosphate phosphatase in Saccharomyces cerevisiae.
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...
متن کاملRegulation of repressible acid phosphatase gene transcription in Saccharomyces cerevisiae.
We examined the genetic system responsible for transcriptional regulation of repressible acid phosphatase (APase; orthophosphoric-monoester phosphohydrolase [acid optimum, EC 3.1.3.2]) in Saccharomyces cerevisiae at the molecular level by analysis of previously isolated and genetically well-defined regulatory gene mutants known to affect APase expression. These mutants identify numerous positiv...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1988
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.170.8.3561-3566.1988