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

Jacob T. Bush, Robert K. Leśniak, Tzu Lan Yeh, Roman Belle, Holger Kramer, Anthony Tumber, Rasheduzzaman Chowdhury, Emily Flashman, Jasmin Mecinović*, Christopher J. Schofield

*Kontaktforfatter for dette arbejde

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Abstrakt

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.

OriginalsprogEngelsk
TidsskriftChemical Communications
Vol/bind55
Udgave nummer8
Sider (fra-til)1020-1023
ISSN1359-7345
DOI
StatusUdgivet - 25. jan. 2019

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