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J Biol Chem, Vol. 273, Issue 10, 5447-5450, March 6, 1998
-Carboxylation by a
Vitamin K-dependent Carboxylase from a Conus
Snail
,,,
, and
From the Departments of Conantokin-G isolated from the marine snail
Conus geographus is a 17-amino acid Biology and Pathology,
University of Utah, Salt Lake City, Utah 84112 and ¶ Cognetix
Inc., Salt Lake City, Utah 84108
-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, -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 -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 -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 -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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