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Cleavage of farnesylated COOH-terminal heptapeptide of mouse N-ras by brain microsomal membranes: Evidence for a carboxypeptidase which specifically removes the COOH-terminal methionine

Cleavage of farnesylated COOH-terminal heptapeptide of mouse N-ras by brain microsomal membranes: Evidence for a carboxypeptidase which specifically removes the COOH-terminal methionine

Biochemical and Biophysical Research Communications 187(3): 1336-1342

Brain microsomal membranes are capable of sequentially removing Met, Leu and Val from a chemically synthesized COOH-terminal heptapeptide (propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met) of mouse N-ras protein. The carboxypeptidase generating Met displays maximum activity at neutral pH and shows high affinity for the farnesylated substrate (Km = 73 microM) as compared to its non farnesylated precursor (Km = 600 microM). The results of inhibitor action suggest that the membrane carboxypeptidase is a novel, probably thiol-dependent, serine type peptidase.

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Accession: 008322377

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PMID: 1417809

DOI: 10.1016/0006-291x(92)90449-u

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