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Changing glycine 21 for glutamic acid in the beta-subunit of penicillin G acylase from Kluyvera citrophila prevents protein maturation.

Abstract：

:Active penicillin acylase from Kluyvera citrophila strain ATCC 21,285 consists of two different alpha- and beta-subunits derived from a single precursor by post-translational processing. Using the chemical mutagen hydroxylamine we have treated plasmid pYKD59 containing the active penicillin acylase gene (pga) from K. citrophila and have generated different point mutant penicillin acylase genes, one producing a maturation deficient precursor. This point mutation has changed the glycine 310 residue of the precursor for a glutamic acid (residue number 21 of the mature beta-subunit). The introduction of a charged residue in this position did not prevent translocation of the precursor to the periplasm but the resultant molecule was not able to undergo subsequent post-translational modification to yield the active protein.

journal_name

Appl Microbiol Biotechnol

journal_title

Applied microbiology and biotechnology

authors

Prieto I,Rodríguez MC,Márquez G,Pérez-Aranda A,Barbero JL

doi

10.1007/BF00183245

subject

Has Abstract

pub_date

1992-02-01 00:00:00

pages

659-62

issue

5

eissn

0175-7598

issn

1432-0614

journal_volume

36

pub_type

杂志文章

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