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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1998-4-7
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pubmed:abstractText |
Conantokin-G isolated from the marine snail Conus geographus is a 17-amino acid gamma-carboxyglutamate (Gla)-containing peptide that inhibits the N-methyl-D-aspartate receptor. We describe the cloning and sequence of conantokin-G cDNA and the possible role of the propeptide sequence. The cDNA encodes a 100amino acid peptide. The N-terminal 80 amino acids constitute the prepro-sequence, and the mature peptide is derived from the remaining C-terminal residues after proteolysis, C-terminal amidation, and a unique post-translational modification, gamma-carboxylation of glutamate residues to Gla. Mature conantokin-G peptide containing Glu residues (E.Con-G) in place of Gla is a poor substrate for the vitamin K-dependent gamma-glutamyl carboxylase (apparent Km = 3.4 mM). Using peptides corresponding to different segments of the propeptide we investigated a potential role for the propeptide sequences in gamma-carboxylation. Propeptide segment -20 to -1 covalently linked to E.Con-G or the synthetic pentapeptide FLEEL increased their apparent affinities 2 orders of magnitude. These substrates are not efficiently carboxylated by the bovine microsomal gamma-glutamyl carboxylase, suggesting differences in specificities between the Conus and the mammalian enzyme. However, the role of propeptide in enhancing the efficiency of carboxylation is maintained.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/1-Carboxyglutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Carbon Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Conotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Excitatory Amino Acid Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Mollusk Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/conotoxin GV,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl carboxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5447-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9488665-1-Carboxyglutamic Acid,
pubmed-meshheading:9488665-Amino Acid Sequence,
pubmed-meshheading:9488665-Animals,
pubmed-meshheading:9488665-Base Sequence,
pubmed-meshheading:9488665-Carbon-Carbon Ligases,
pubmed-meshheading:9488665-Cattle,
pubmed-meshheading:9488665-Cloning, Molecular,
pubmed-meshheading:9488665-Conotoxins,
pubmed-meshheading:9488665-Excitatory Amino Acid Antagonists,
pubmed-meshheading:9488665-Glutamic Acid,
pubmed-meshheading:9488665-Kinetics,
pubmed-meshheading:9488665-Microsomes,
pubmed-meshheading:9488665-Molecular Sequence Data,
pubmed-meshheading:9488665-Mollusk Venoms,
pubmed-meshheading:9488665-Peptide Fragments,
pubmed-meshheading:9488665-Peptides, Cyclic,
pubmed-meshheading:9488665-Protein Precursors,
pubmed-meshheading:9488665-Protein Processing, Post-Translational,
pubmed-meshheading:9488665-Sequence Analysis, DNA,
pubmed-meshheading:9488665-Snails,
pubmed-meshheading:9488665-Substrate Specificity
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pubmed:year |
1998
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pubmed:articleTitle |
Conantokin-G precursor and its role in gamma-carboxylation by a vitamin K-dependent carboxylase from a Conus snail.
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pubmed:affiliation |
Department of Biology, University of Utah, Salt Lake City, Utah 84112, USA. bandyop@biology.utah.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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