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A molecular mechanism for the enzymatic methylation of nitrogen atoms within peptide bonds

Abstract:

The peptide bond, the defining feature of proteins, governs peptide chemistry by abolishing nucleophilicity of the nitrogen. This and the planarity of the peptide bond arise from the delocalization of the lone pair of electrons on the nitrogen atom into the adjacent carbonyl. While chemical methylation of an amide bond uses a strong base to generate the imidate, OphA, the precursor protein of the fungal peptide macrocycle omphalotin A, self-hypermethylates amides at pH 7 using S-adenosyl meth...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1126/sciadv.aat2720

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Structural Biology
Role:
Author
ORCID:
0000-0002-7568-0544
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Role:
Author
ORCID:
0000-0003-3516-3507
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Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/R018189/1
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Name:
European Research Council
Grant:
NCB-TNT 339367
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Name:
Swiss National Science Foundation
Grant:
200021–159713
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Name:
Wellcome Trust
Grant:
094476/Z/10/Z
Publisher:
American Association for the Advancement of Science
Journal:
Science Advances More from this journal
Volume:
4
Issue:
8
Article number:
eaat2720
Publication date:
2018-08-24
Acceptance date:
2018-07-17
DOI:
ISSN:
2375-2548
Pmid:
30151425
Language:
English
Pubs id:
pubs:911604
UUID:
uuid:d051ec44-9afa-4b22-933b-2888d309eb80
Local pid:
pubs:911604
Source identifiers:
911604
Deposit date:
2018-09-11

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