JMJD5 is a human arginyl C-3 hydroxylase

Sarah E. Wilkins; Md. Saiful Islam; Joan M. Gannon; Suzana Markolovic; Richard J. Hopkinson; Wei Ge; Christopher J. Schofield; Rasheduzzaman Chowdhury

doi:10.1038/s41467-018-03410-w

Nature Communications (Mar 2018)

JMJD5 is a human arginyl C-3 hydroxylase

Sarah E. Wilkins,
Md. Saiful Islam,
Joan M. Gannon,
Suzana Markolovic,
Richard J. Hopkinson,
Wei Ge,
Christopher J. Schofield,
Rasheduzzaman Chowdhury

Affiliations

Sarah E. Wilkins: The Department of Chemistry, University of Oxford
Md. Saiful Islam: The Department of Chemistry, University of Oxford
Joan M. Gannon: The Department of Chemistry, University of Oxford
Suzana Markolovic: The Department of Chemistry, University of Oxford
Richard J. Hopkinson: The Department of Chemistry, University of Oxford
Wei Ge: The Department of Chemistry, University of Oxford
Christopher J. Schofield: The Department of Chemistry, University of Oxford
Rasheduzzaman Chowdhury: The Department of Chemistry, University of Oxford

DOI: https://doi.org/10.1038/s41467-018-03410-w
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 12

Abstract

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Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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