Cargando…
Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6
JmjC domain-containing protein 6 (JMJD6) is a 2-oxoglutarate (2OG)-dependent oxygenase linked to various cellular processes, including splicing regulation, histone modification, transcriptional pause release, hypoxia sensing, and cancer. JMJD6 is reported to catalyze hydroxylation of lysine residue(...
Autores principales: | Islam, Md. Saiful, McDonough, Michael A., Chowdhury, Rasheduzzaman, Gault, Joseph, Khan, Amjad, Pires, Elisabete, Schofield, Christopher J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6663879/ https://www.ncbi.nlm.nih.gov/pubmed/31147442 http://dx.doi.org/10.1074/jbc.RA119.008693 |
Ejemplares similares
-
Structural analysis of the 2-oxoglutarate binding site of the circadian rhythm linked oxygenase JMJD5
por: Islam, Md. Saiful, et al.
Publicado: (2022) -
Inhibition of JMJD6 by 2‐Oxoglutarate Mimics
por: Islam, Md. Sailful, et al.
Publicado: (2021) -
Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii
por: Liu, Tongri, et al.
Publicado: (2021) -
JMJD5 is a human arginyl C-3 hydroxylase
por: Wilkins, Sarah E., et al.
Publicado: (2018) -
The mechanism of a one-substrate transketolase reaction
por: Solovjeva, Olga N., et al.
Publicado: (2020)