Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Christopher J. Schofield"'
Publikováno v:
Scientific reports. 12(1)
JmjC (Jumonji-C) domain-containing 5 (JMJD5) plays important roles in circadian regulation in plants and humans and is involved in embryonic development and cell proliferation. JMJD5 is a 2-oxoglutarate (2OG) and Fe(II) dependent oxygenase of the Jmj
Autor:
Christopher J. Schofield, Eidarus Salah, Lennart Brewitz, Armin Thalhammer, Anthony Tumber, Kirsten E. Christensen
Publikováno v:
Chemmedchem
The human 2‐oxoglutarate (2OG)‐dependent oxygenase aspartate/asparagine‐β‐hydroxylase (AspH) is a potential medicinal chemistry target for anticancer therapy. AspH is present on the cell surface of invasive cancer cells and accepts epidermal
Publikováno v:
Natural Product Reports
The 2OG oxygenases and IPNS contribute to the great structural diversity of β-lactam natural products, employing some remarkable mechanisms.
Covering: up to 2017 2-Oxoglutarate (2OG) dependent oxygenases and the homologous oxidase isopenicillin
Covering: up to 2017 2-Oxoglutarate (2OG) dependent oxygenases and the homologous oxidase isopenicillin
Autor:
Michael A. McDonough, S.S. Ng, Christopher J. Schofield, Grazyna Kochan, Kathryn L. Kavanagh, Zhihong Zhang, Udo Oppermann
Publikováno v:
Biochemical and Biophysical Research Communications. 408:553-558
Phytanoyl-CoA hydroxylase (PAHX) catalyzes an important step in the metabolism of the fatty acid side chain of chlorophyll. PHYHD1 exists in three isoforms and is the closest human homologue of PAHX. We show that like PAHX, the PHYHD1A but likely not
Publikováno v:
Chemistry & Biology. 16(6):580-583
Recent reports identify the oxygenase catalyzed production of 5-hydroxymethylcytosine as a modification to mammalian DNA (Kriaucionis and Heintz, 2009; Tahiliani et al., 2009). This discovery has potential far-reaching implications for epigenetic reg
Autor:
Atsushi Yamamoto, Marion S. Schmidt-Zachmann, Armin Thalhammer, Ming Yang, Gail M. Preston, James S. O. McCullagh, Alexander Wolf, Chia Hua Ho, Phebee Liu-Yi, Adam P. Hardy, Zhihong Zhang, Peter J. Ratcliffe, Adam Zayer, Carol V. Robinson, Tianshu Feng, Benedikt M. Kessler, Nikita D. Loik, Mathew L. Coleman, Rok Sekirnik, Timothy D. W. Claridge, Muhammad Mukram Mohamed Mackeen, Refaat B. Hamed, Miao Jiang, Matthew E. Cockman, Rasheduzzaman Chowdhury, Christoph Loenarz, Christopher J. Schofield, David C. Trudgian, Nicolas Granatino, Wei Ge, Yuliya Gordiyenko, Lingzhi Gong
Publikováno v:
Nature chemical biology. 8(12)
The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxogl
Publikováno v:
The FEBS journal. 279(9)
Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, whic
Publikováno v:
Analytical biochemistry. 336(1)
A widely used generic assay for 2-oxoglutarate-dependent oxygenases relies upon monitoring the release of 14CO2 from labeled [1-14C]-2-oxoglutarate. We report an alternative assay in which depletion of 2-oxoglutarate is monitored by its postincubatio
Autor:
Jonathan J, Turnbull, Jun-Ichiro, Nakajima, Richard W D, Welford, Mami, Yamazaki, Kazuki, Saito, Christopher J, Schofield
Publikováno v:
The Journal of biological chemistry. 279(2)
Anthocyanidin synthase (ANS), flavonol synthase (FLS), and flavanone 3beta-hydroxylase (FHT) are involved in the biosynthesis of flavonoids in plants and are all members of the family of 2-oxoglutarate- and ferrous iron-dependent oxygenases. ANS, FLS