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Small-molecules that covalently react with a human prolyl hydroxylase – towards activity modulation and substrate capture

Abstract:
We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.1039/C8CC07706A

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Oxford college:
Pembroke College
Role:
Author
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Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
55
Issue:
8
Pages:
1020-1023
Publication date:
2018-11-19
Acceptance date:
2018-11-01
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:936513
URN:
uri:3fcef202-cb23-4209-8d01-7298411b874a
UUID:
uuid:3fcef202-cb23-4209-8d01-7298411b874a
Local pid:
pubs:936513

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