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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2000-8-17
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pubmed:abstractText |
A calcium- and phospholipid-dependent protein kinase of apparent molecular mass 54 kDa (designated ZmCPKp54) was partially purified from etiolated maize seedlings. Activity of ZmCPKp54 is stimulated by phosphatidylserine and phosphatidylinositol, but is not essentially affected by diolein and phorbol esters. The enzyme cross-reacts with polyclonal antibodies against the calmodulin like-domain of the calcium-dependent protein kinase, but not with antibodies against catalytic or regulatory domains of protein kinase C. ZmCPKp54 is not able to phosphorylate the specific substrates of protein kinase C (MARCKS peptide and protein kinase C substrate peptide derived from pseudosubstrate sequence) and its activity is not inhibited by specific PKC inhibitors (bisindolylmaleimide, protein kinase C pseudosubstrate inhibitory peptide). The substrate specificity and sensitivity to the inhibitors of the maize enzyme resembles calcium-dependent protein kinase. The biochemical and immunological properties indicate that ZmCPKp54 belongs to the calcium-dependent protein kinase family.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/calcium-dependent protein kinase,
http://linkedlifedata.com/resource/pubmed/chemical/myristoylated alanine-rich C...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3818-27
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10849001-Amino Acid Sequence,
pubmed-meshheading:10849001-Calcium,
pubmed-meshheading:10849001-Cross Reactions,
pubmed-meshheading:10849001-Egtazic Acid,
pubmed-meshheading:10849001-Enzyme Activation,
pubmed-meshheading:10849001-Enzyme Inhibitors,
pubmed-meshheading:10849001-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10849001-Isoenzymes,
pubmed-meshheading:10849001-Membrane Proteins,
pubmed-meshheading:10849001-Molecular Sequence Data,
pubmed-meshheading:10849001-Molecular Weight,
pubmed-meshheading:10849001-Peptide Fragments,
pubmed-meshheading:10849001-Phospholipids,
pubmed-meshheading:10849001-Protein Kinases,
pubmed-meshheading:10849001-Proteins,
pubmed-meshheading:10849001-Seeds,
pubmed-meshheading:10849001-Substrate Specificity,
pubmed-meshheading:10849001-Zea mays
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pubmed:year |
2000
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pubmed:articleTitle |
Calcium-dependent protein kinase from maize seedlings activated by phospholipids.
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pubmed:affiliation |
Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warszawa, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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