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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
39
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pubmed:dateCreated |
2004-9-20
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pubmed:abstractText |
Hepatic carnitine palmitoyltransferase-I (CPT-IL) isolated from mitochondrial outer membranes obtained in the presence of protein phosphatase inhibitors is readily recognized by phosphoamino acid antibodies. Mass spectrometric analysis of CPT-IL tryptic digests revealed the presence of three phosphopeptides including one with a protein kinase CKII (CKII) consensus site. Incubation of dephosphorylated outer membranes with protein kinases and [gamma-32P]ATP resulted in radiolabeling of CPT-I only by CKII. Using mass spectrometry, only one region of phosphorylation was detected in CPT-I isolated from CKII-treated mitochondria. The sequence of the peptide and position of phosphorylated amino acids have been determined unequivocally as FpSSPETDpSHRFGK (residues 740-752). Furthermore, incubation of dephosphorylated outer membranes with CKII and unlabeled ATP led to increased catalytic activity and rendered malonyl-CoA inhibition of CPT-I from competitive to uncompetitive. These observations identify a new mechanism for regulation of hepatic CPT-I by phosphorylation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.
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pubmed:issnType |
Print
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pubmed:day |
24
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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 |
41104-13
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15247243-Amino Acid Sequence,
pubmed-meshheading:15247243-Animals,
pubmed-meshheading:15247243-Binding, Competitive,
pubmed-meshheading:15247243-Carnitine O-Palmitoyltransferase,
pubmed-meshheading:15247243-Casein Kinase II,
pubmed-meshheading:15247243-Cell Membrane,
pubmed-meshheading:15247243-Dose-Response Relationship, Drug,
pubmed-meshheading:15247243-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15247243-Immunoblotting,
pubmed-meshheading:15247243-Ions,
pubmed-meshheading:15247243-Kinetics,
pubmed-meshheading:15247243-Liver,
pubmed-meshheading:15247243-Male,
pubmed-meshheading:15247243-Malonyl Coenzyme A,
pubmed-meshheading:15247243-Mass Spectrometry,
pubmed-meshheading:15247243-Mitochondria, Liver,
pubmed-meshheading:15247243-Molecular Sequence Data,
pubmed-meshheading:15247243-Peptides,
pubmed-meshheading:15247243-Phosphorylation,
pubmed-meshheading:15247243-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15247243-Rats,
pubmed-meshheading:15247243-Rats, Sprague-Dawley,
pubmed-meshheading:15247243-Sequence Homology, Amino Acid,
pubmed-meshheading:15247243-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15247243-Trypsin
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pubmed:year |
2004
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pubmed:articleTitle |
Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase-I: effect on the kinetic properties of the enzyme.
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pubmed:affiliation |
Department of Nutrition, Biochemistry, and Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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