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Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases

Abstract:

The Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene expression and protein biosynthesis. Human JmjC 2OG oxygenases catalyze oxidative modifications to give either chemically stable alcohol products, or in the case of N(ɛ)-methyl lysine demethylation, relatively unstable hemiaminals that fragment to give formaldehyde and the demethylated product. Recent work has yielded conflicting reports as to...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.sbi.2016.05.013

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Oxford Ludwig Institute
Role:
Author
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Biotechnology and Biological Sciences Research Council More from this funder
Wellcome Trust More from this funder
Cancer Research UK More from this funder
Ludwig Institute for Cancer Research More from this funder
Engineering and Physical Sciences Research Council More from this funder
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Publisher:
Elsevier Publisher's website
Journal:
Current opinion in structural biology Journal website
Volume:
41
Pages:
62-72
Publication date:
2016-06-14
DOI:
EISSN:
1879-033X
ISSN:
0959-440X
URN:
uuid:8cf46d5d-9d37-4b2b-8e67-536f8ea5cd38
Source identifiers:
628635
Local pid:
pubs:628635
Language:
English

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