Please use this identifier to cite or link to this item: https://doi.org/10.1139/cjm-47-10-961
Title: Mutational analysis of conserved glycines 42 and 256 in Cephalosporium acremonium isopenicillin N synthase
Authors: Loke, P. 
Sim, T.-S. 
Keywords: Cephalosporium acremonium
Glycine
Isopenicillin N synthase
Site-directed mutagenesis
Issue Date: 2001
Source: Loke, P., Sim, T.-S. (2001). Mutational analysis of conserved glycines 42 and 256 in Cephalosporium acremonium isopenicillin N synthase. Canadian Journal of Microbiology 47 (10) : 961-964. ScholarBank@NUS Repository. https://doi.org/10.1139/cjm-47-10-961
Abstract: Isopenicillin N synthase (IPNS) is critical for the catalytic conversion of δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine to isopenicillin N in the penicillin and cephalosporin biosynthetic pathway. Two conserved glycine residues in Cephalosporium acremonium IPNS (cIPNS), namely glycine-42 and glycine-256, were identified by multiple sequence alignment and investigated by site-directed mutagenesis to study the effect of the substitution on catalysis. Our study showed that both the mutations from glycine to alanine or to serine reduced the catalytic activity of cIPNS and affected its soluble expression in a heterologous host at 37°C. Soluble expression was restored at a reduced temperature of 25°C, and thus, it is possible that these glycine residues may have a role in maintaining the local protein structure and are critical for the soluble expression of cIPNS.
Source Title: Canadian Journal of Microbiology
URI: http://scholarbank.nus.edu.sg/handle/10635/131269
ISSN: 00084166
DOI: 10.1139/cjm-47-10-961
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

1
checked on Jan 17, 2018

Page view(s)

6
checked on Jan 21, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.