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 Nɛ-methyl lysine demethylation, relatively unstable hemiaminals that fragment to give formaldehyde and the demethylated product. Recent work has yielded conflicting reports as to whether some JmjC oxygenases catalyze N-methyl group demethylation or hydroxylation reactions. We review JmjC oxygenase-catalyzed reactions within the context of structural knowledge, highlighting key differences between hydroxylases and demethylases, which have the potential to inform on the possible type(s) of reactions catalyzed by partially characterized or un-characterized JmjC oxygenases in humans and other organisms.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Markolovic S,Leissing TM,Chowdhury R,Wilkins SE,Lu X,Schofield CJdoi
10.1016/j.sbi.2016.05.013subject
Has Abstractpub_date
2016-12-01 00:00:00pages
62-72eissn
0959-440Xissn
1879-033Xpii
S0959-440X(16)30048-3journal_volume
41pub_type
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journal_title：Current opinion in structural biology
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