Article
Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft.
Journal of molecular biology - 29 Sept 2000
Hewitt L, Kasche V, Lummer K, Lewis R J, Murshudov G N, Verma C S, Dodson G G, Wilson K S
Abstract excerpt
Penicillin G acylase is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme (209 and 557 residues respectively) joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm. The first step in processing is believed to be...
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