Structure-function relationships in KDM7 histone demethylases.

Authors

Shobhit Chaturvedi, Michigan Technological UniversityFollow
Rajeev Ramanan, Michigan Technological UniversityFollow
Sodiq Waheed, Michigan Technological UniversityFollow
Tatyana Karabencheva-Christova, Michigan Technological UniversityFollow
Christo Christov, Michigan Technological University

Document Type

Article

Publication Date

2019

Department

Department of Chemistry

Abstract

The demethylation of lysine residues of histone proteins is a key epigenetic mechanism in cells. The enzymes that catalyze these processes are called histone demethylases (KDMs). The largest family of KDMs is the Jumonji C (JmjC) domain-containing enzymes; these includes KDM2-7 subfamily of enzymes. The JmjC proteins are Fe(II) and 2-Oxoglutarate (2OG) - dependent dioxygenases that couple substrate oxidation to decarboxylation of 2OG to form succinate and CO

Publisher's Statement

Copyright © 2019 Elsevier Inc. All rights reserved. Publisher’s version of record: https://doi.org/10.1016/bs.apcsb.2019.08.005

Publication Title

Adv Protein Chem Struct Biol

Recommended Citation

Chaturvedi, S., Ramanan, R., Waheed, S., Karabencheva-Christova, T., & Christov, C. (2019). Structure-function relationships in KDM7 histone demethylases.. Adv Protein Chem Struct Biol, 117, 113-125. http://doi.org/10.1016/bs.apcsb.2019.08.005
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/846