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Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105

Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia... The two constituent subunits of the enzyme penicillin acylase from Escherichia coli strain ATCC 11105 are derived from a single precursor polypeptide by post‐translational processing. Mutant penicillin acylase precursors were constructed carrying insertions and deletions in various domains and they were analysed for their processing behaviour. It was found that an endopeptide region of appropriate size and an intact C‐terminus were absolutely necessary for the maturation process. Internal deletions within the β‐subunit domain also prevented post‐translational cleavage. Processing competence, therefore, was not merely determined by the amino acid sequence in the vicinity of the processing sites but relied on a correct overall conformation of the protein. The processing pathway in vivo proceeds via an intermediate comprising the α subunits plus endopeptide and is thus identical to the pathway which has been determined previously by in vitro analysis. The post‐translational modification of the precursor is probably not carried out by a specific processing enzyme(s) as the heterologous expression of the penicillin acylase (pac) structural gene yielded processed and active enzyme in different enterobacteria and in a Pseudomonas species. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Febs Journal Wiley

Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105

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References (32)

Publisher
Wiley
Copyright
Copyright © 1990 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1742-464X
eISSN
1742-4658
DOI
10.1111/j.1432-1033.1990.tb19207.x
Publisher site
See Article on Publisher Site

Abstract

The two constituent subunits of the enzyme penicillin acylase from Escherichia coli strain ATCC 11105 are derived from a single precursor polypeptide by post‐translational processing. Mutant penicillin acylase precursors were constructed carrying insertions and deletions in various domains and they were analysed for their processing behaviour. It was found that an endopeptide region of appropriate size and an intact C‐terminus were absolutely necessary for the maturation process. Internal deletions within the β‐subunit domain also prevented post‐translational cleavage. Processing competence, therefore, was not merely determined by the amino acid sequence in the vicinity of the processing sites but relied on a correct overall conformation of the protein. The processing pathway in vivo proceeds via an intermediate comprising the α subunits plus endopeptide and is thus identical to the pathway which has been determined previously by in vitro analysis. The post‐translational modification of the precursor is probably not carried out by a specific processing enzyme(s) as the heterologous expression of the penicillin acylase (pac) structural gene yielded processed and active enzyme in different enterobacteria and in a Pseudomonas species.

Journal

The Febs Journal – Wiley

Published: Aug 1, 1990

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