Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66-Reference-Cited by-同舟云学术

Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66

Published:2023 Issue:3 Volume:4 Page:235-243
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Türkmen Vildan A.¹,Hintzen Jordi C. J.¹^ORCID,Tumber Anthony²,Moesgaard Laust¹,Salah Eidarus²,Kongsted Jacob¹^ORCID,Schofield Christopher J.²^ORCID,Mecinović Jasmin¹^ORCID

Affiliation:

1. Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark

2. Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, OX1 3TA Oxford, UK

Abstract

Ribosomal histidine hydroxylases MINA53 and NO66 exhibit narrow substrate selectivities for ribosomal protein L27a/L8 peptides possessing histidine analogues. Selected Rpl peptides display potent inhibition against MINA53 and NO66, providing a basis for inhibitor design.

Funder

H2020 European Research Council

Wellcome Trust

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CB/D2CB00182A

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