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J. Biol. Chem., Vol. 262, Issue 32, 15334-15337, 11, 1987
JE Knobloch and JW Suttie
A liver microsomal enzyme catalyzes the vitamin K-dependent
posttranslational carboxylation of specific glutamyl residues of a limited
number of plasma proteins to gamma-carboxyglutamyl residues. The
intracellular precursor forms of these proteins are known to contain a
homologous basic amino acid-rich propeptide region between the signal
peptide region and the amino terminus of the mature protein. This region of
the precursor protein has been implicated as a possible recognition site
for the carboxylase enzyme. A 20-residue peptide containing the
octadecapropeptide of human clotting factor X has now been shown to
strongly stimulate the activity of the enzyme toward a noncovalently linked
substrate. This stimulatory effect is seen at less than micromolar
concentrations and is accompanied by a decrease in the Km of the glutamic
acid substrate. These observations raise the possibility that the catalytic
activity of other enzymes involved in protein processing may be regulated
by a portion of their normal substrates.
Vitamin K-dependent carboxylase. Control of enzyme activity by the "propeptide" region of factor X
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
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