Journal article icon

Journal article

The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.

Abstract:

Isopenicillin N synthase (IPNS) catalyses cyclization of δ-(l-α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN), the central step in penicillin biosynthesis. Previous studies have shown that IPNS turns over a wide range of substrate analogues in which the valine residue of its natural substrate is replaced with other amino acids. IPNS accepts and oxidizes numerous substrates that bear hydrocarbon sidechains in this position, however the enzyme is less tolerant of analogues p...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1016/j.abb.2011.09.014

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Journal:
Archives of biochemistry and biophysics
Volume:
516
Issue:
2
Pages:
103-107
Publication date:
2011-12-01
DOI:
EISSN:
1096-0384
ISSN:
0003-9861
Source identifiers:
193277
Language:
English
Keywords:
Pubs id:
pubs:193277
UUID:
uuid:2633c46b-9a4b-4541-b067-058aee29b118
Local pid:
pubs:193277
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP