Please use this identifier to cite or link to this item:
|Title:||Analysis of a conserved arginine R281L in catalysis in Cephalosporium acremonium isopenicillin N synthase||Authors:||Loke, P.
Isopenicillin N synthase
|Issue Date:||1998||Citation:||Loke, P.,Sim, T.-S. (1998). Analysis of a conserved arginine R281L in catalysis in Cephalosporium acremonium isopenicillin N synthase. FEMS Microbiology Letters 164 (1) : 107-110. ScholarBank@NUS Repository. https://doi.org/10.1016/S0378-1097(98)00204-3||Abstract:||Isopenicillin N synthase is essential for the catalytic transformation of a linear tripeptide substrate δ-(L-α-aminoadipyl)-Lcysteinyl-D-valine to isopenicillin N in the biosynthesis of β-lactam antibiotics. The recent Aspergillus nidulans isopenicillin N synthase crystal structure proposed that a conserved arginine, R279, has a role in substrate binding. This study, the first site-directed mutagenesis experiment on arginine in isopenicillin N synthase, was carried out to ascertain the role of the similarly conserved and corresponding arginine residue R281 on catalysis in the fungal Cephalosporium acremonium isopenicillin N synthase. Replacement of the arginine residue with leucine to generate the mutant R281L Cephalosporium isopenicillin N synthase resulted in undetectable activity as shown by enzyme bioassays. It is possible that the mutant's substrate binding capability was eliminated, thus preventing the catalytic reaction. Further investigation into the corresponding arginine residues in isopenicillin N synthase of other species is warranted.||Source Title:||FEMS Microbiology Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/31096||ISSN:||03781097||DOI:||10.1016/S0378-1097(98)00204-3|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Apr 20, 2019
checked on Mar 17, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.