Title: Structure of the penicillin acylase gene from Escherichia coli: a periplasmic enzyme that undergoes multiple proteolytic processing. | Journal: Journal of molecular and applied genetics. 1985 ;3(1):36-44 | Authors: Bruns W, Hoppe J, Tsai H, BrĂ¼ning HJ, Maywald F, Collins J, Mayer H. | Abstract: Penicillin acylase is processed from a 90-kD precursor through the cleavage of a leader peptide and two further endopeptidase cleavages to yield an enzyme that contains a 22-kD (or 23-kD) and a 65-kD subunit. The endopeptidase cleavages require an intact carboxy terminus. This type of processing appears to be unique for a prokaryotic enzyme, having its most closely related analog in the synthesis and processing of preproinsulin and other eukaryotic hormones. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/2989404 |
|