Peptides from the venom ducts of cone snails (genus Coitus) contain ga
mma-carboxyglutamate residues. The gamma-glutamyl carboxylase responsi
ble for this post-translational modification is localized in the micro
somal fraction, strictly dependent on vitamin It, activated by ammoniu
m sulfate, and is associated with endogenous substrate. The K-m of the
enzyme for vitamin K is comparable to that for the bovine carboxylase
, However, a propeptide containing substrate related to the blood coag
ulation protein factor IX, a highly efficient substrate for the bovine
enzyme, was poorly carboxylated by the Conus enzyme, suggesting diffe
rences in gamma-carboxylase recognition signal sequences and/or struct
ural requirements at the carboxylation site. (C) 1997 Federation of Eu
ropean Biochemical Societies.