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Heterologous expression of leader-less pga gene in Pichia pastoris: intracellular production of prokaryotic enzyme.

Helena Maresova, Zdena Markova, Renata Valesova, Jan Sklenar, and Pavel Kyslik

BMC Biotechnol (2010) PMID 20128906

Penicillin G acylase of Escherichia coli (PGAEc) is a commercially valuable enzyme for which efficient bacterial expression systems have been developed. The enzyme is used as a catalyst for the hydrolytic production of beta-lactam nuclei or for the synthesis of semi-synthetic penicillins such as ampicillin, amoxicillin and cephalexin. To become a mature, periplasmic enzyme, the inactive prepropeptide of PGA has to undergo complex processing that begins in the cytoplasm (autocatalytic cleavage), continues at crossing the cytoplasmic membrane (signal sequence removing), and it is completed in the periplasm. Since there are reports on impressive cytosolic expression of bacterial proteins in Pichia, we have cloned the leader-less gene encoding PGAEc in this host and studied yeast production capacity and enzyme authenticity.

DOI: 10.1186/1472-6750-10-7
Version: za2963e q8zae q8zbb q8zc5 q8zde q8zec q8zfa q8zg6
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