E-mail a Wiley Online Library Link

Dr. Adam Daruzzaman, Dr. Ian J. Clifton, Dr. Robert M. Adlington, Prof. Sir Jack E. Baldwin and Dr. Peter J. Rutledge The Interaction of Isopenicillin N Synthase with Homologated Substrate Analogues δ-(L-α-Aminoadipoyl)-L-homocysteinyl-D-Xaa Characterised by Protein Crystallography ChemBioChem 14

Version of Record online: 6 MAR 2013 | DOI: 10.1002/cbic.201200728

Thumbnail image of graphical abstract

Loose fit: IPNS catalyses the central step in penicillin biosynthesis. Substrate analogues containing L-homocysteine in place of the natural substrate's L-cysteine residue are not converted into bicyclic products. Crystal structures for IPNS complexes with two such analogues reveal that the additional CH2 unit affords considerable conformational freedom when these analogues bind to IPNS.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field