Terminally Truncated Isopenicillin N Synthase Generates a Dithioester Product: Evidence for a Thioaldehyde Intermediate during Catalysis and a New Mode of Reaction for Non-Heme Iron Oxidases-Reference-Cited by-同舟云学术

Terminally Truncated Isopenicillin N Synthase Generates a Dithioester Product: Evidence for a Thioaldehyde Intermediate during Catalysis and a New Mode of Reaction for Non-Heme Iron Oxidases

Published:2017-08-21 Issue:52 Volume:23 Page:12815-12824
ISSN:0947-6539
Container-title:Chemistry - A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

McNeill Luke A.¹²,Brown Toby J. N.¹³,Sami Malkit¹⁴,Clifton Ian J.¹,Burzlaff Nicolai I.⁵,Claridge Timothy D. W.¹,Adlington Robert M.¹,Baldwin Jack E.¹,Rutledge Peter J.⁶^ORCID,Schofield Christopher J.¹

Affiliation:

1. Oxford Centre for Molecular Sciences and the Department of Chemistry; Chemistry Research Laboratory; Mansfield Road Oxford OX1 3TA UK

2. Present Address: Oxford Nanopore Technologies, Oxford Science Park; OX4 4GA UK

3. Present Address: The Brattle Group; Level 15 5 Martin Place Sydney, NSW 2000 Australia

4. Present Address: Immunocore Limited; 101 Park Drive, Milton Park Abingdon OX14 4RY UK

5. Department of Chemistry and Pharmacy; University of Erlangen-Nuremberg; Egerlandstraße 1 91058 Erlangen Germany

6. School of Chemistry; The University of Sydney, NSW; 2006 Australia

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Reference68 articles.

1. The enzymes of β-lactam biosynthesis

2. Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology

3. Highly Selective but Multifunctional Oxygenases in Secondary Metabolism

4. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

5. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

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