Source:http://linkedlifedata.com/resource/pubmed/id/14630917
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2004-2-9
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| pubmed:abstractText |
The Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase is a vacuole membrane-associated enzyme that catalyzes the removal of the beta-phosphate from diacylglycerol pyrophosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol. The enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity. In this work, we examined the topography of diacylglycerol-pyrophosphate phosphatase catalytic site within the transverse plane of the vacuole membrane. Results of protease protection analysis using endoproteinase Lys-C and labeling of cysteine residues using sulfhydryl reagents were consistent with a model where the catalytic site of diacylglycerol-pyrophosphate phosphatase was oriented to the cytosolic face of the vacuole membrane. In addition, diacylglycerol-pyrophosphate phosphatase activity was found with intact vacuoles. The phospholipids diacylglycerol pyrophosphate (0.6 mol %) and phosphatidate (1.4 mol %) were found in the vacuole membrane, and their levels decreased to an undetectable level and by 79%, respectively, when cells were depleted for zinc. The reduced levels of diacylglycerol pyrophosphate and phosphatidate correlated with the induced expression of diacylglycerol-pyrophosphate phosphatase. This work suggested that diacylglycerol pyrophosphate phosphatase functions to regulate the levels of diacylglycerol pyrophosphate and phosphatidate on the cytosolic face of the vacuole membrane.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrophosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/diacylglycerol pyrophosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/peptidyl-Lys metalloendopeptidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
13
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| pubmed:volume |
279
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5338-45
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14630917-Amino Acid Motifs,
pubmed-meshheading:14630917-Catalytic Domain,
pubmed-meshheading:14630917-Cell Membrane,
pubmed-meshheading:14630917-Cysteine,
pubmed-meshheading:14630917-Cytosol,
pubmed-meshheading:14630917-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14630917-Hydrolysis,
pubmed-meshheading:14630917-Immunoblotting,
pubmed-meshheading:14630917-Metalloendopeptidases,
pubmed-meshheading:14630917-Microscopy, Fluorescence,
pubmed-meshheading:14630917-Models, Biological,
pubmed-meshheading:14630917-Mutation,
pubmed-meshheading:14630917-Peptides,
pubmed-meshheading:14630917-Phospholipids,
pubmed-meshheading:14630917-Protein Structure, Tertiary,
pubmed-meshheading:14630917-Pyrophosphatases,
pubmed-meshheading:14630917-Saccharomyces cerevisiae,
pubmed-meshheading:14630917-Time Factors,
pubmed-meshheading:14630917-Vacuoles,
pubmed-meshheading:14630917-Zinc
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| pubmed:year |
2004
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| pubmed:articleTitle |
Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae.
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| pubmed:affiliation |
Department of Food Science, Rutgers University, New Brunswick, New Jersey 08901, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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