Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Christopher J. Schofield"'
Autor:
Amelia, Brasnett, Inga, Pfeffer, Lennart, Brewitz, Rasheduzzaman, Chowdhury, Yu, Nakashima, Anthony, Tumber, Michael A, McDonough, Christopher J, Schofield
Publikováno v:
Angewandte Chemie (International Ed. in English)
Aspartate/asparagine‐β‐hydroxylase (AspH) is a human 2‐oxoglutarate (2OG) and FeII oxygenase that catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor‐like domains (EGFDs). Unusually, AspH employs two histi
Autor:
Christopher J. Schofield, Inga Pfeffer, Anthony Tumber, Michael A. McDonough, Lennart Brewitz
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
The human 2-oxoglutarate dependent oxygenase aspartate/asparagine-β-hydroxylase (AspH) catalyses the hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains (EGFDs). AspH is upregulated on the surface of malign cancer cells; increa
Autor:
Emily Flashman, Holger B. Kramer, Nikita D. Loik, Christopher J. Schofield, Emily A. Howe, Hanna Tarhonskaya, James S. O. McCullagh, Adam P. Hardy
Publikováno v:
The Journal of Biological Chemistry
Background: The hypoxia-inducible factor (HIF) hydroxylases (FIH and PHDs) regulate hypoxia sensing in animals. Results: FIH·HIF-α reacts faster with O2 than PHD2·HIF-α but slower than FIH·ankyrin complexes. Conclusion: The kinetics of catalysis
Publikováno v:
Chemical Communications (Cambridge, England)
The stereochemistry of human trimethyllysine hydroxylase was determined to be (2S,3S)-3-hydroxy-N ε-trimethyllysine by comparison to asymmetrically synthesised (2S,3R)-3-hydroxy-N ε-trimethyllysine.
N ε-Trimethyllysine hydroxylase (TMLH) cata
N ε-Trimethyllysine hydroxylase (TMLH) cata
Autor:
Suzana, Markolovic, Thomas M, Leissing, Rasheduzzaman, Chowdhury, Sarah E, Wilkins, Xin, Lu, Christopher J, Schofield
Publikováno v:
Current opinion in structural biology. 41
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
Autor:
Eleanor A.L. Bagg, Vasilij Koshkin, Sergey N. Krylov, Svetlana M. Krylova, Christopher J. Schofield
Publikováno v:
Journal of medicinal chemistry. 55(7)
The Escherichia coli (E. coli) AlkB protein and its functional human homologues belong to a subfamily of 2-oxoglutarate (2OG) dependent oxygenases (2OG oxygenases for simplicity) that enable the repair of cytotoxic methylation damage in nucleic acids
Autor:
Emily Flashman, Alexander P. Petrov, Sergey N. Krylov, Anna A. Karkhanina, Jasmin Mecinović, Michael U. Musheev, Kirsty Sarah Hewitson, Svetlana M. Krylova, Christopher J. Schofield
Publikováno v:
Analytical chemistry. 81(14)
N/O-methylation of DNA can be cytotoxic and mutagenic; therefore, enzymes that reverse DNA methylation are essential for organism survival. Several 2-oxoglutarate-dependent oxygenases and methyltransferases that remove a methyl group from a methylate