Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Katharine J. Gibson"'
Autor:
Jahnavi Chandra Prasad, Christopher M. Baron, Krasley Elizabeth A, Yixin Ren, Steven Cary Rothman, Katharine J. Gibson, Lori Ann Maggio-Hall, Kristen J. Kelly, Barbara Rice, Ryan M. Lauchli, Gregory H. Rice, Kerry Hollands, Lisa Anne Laffend, Mark J. Nelson
Publikováno v:
Metabolic engineering. 52
Oligosaccharides present in human breast milk have been linked to beneficial effects on infant health. Inclusion of these human milk oligosaccharides (HMOs) in infant formula can recapitulate these health benefits. As a result, there is substantial c
Publikováno v:
Journal of Bacteriology. 183:6478-6486
Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able
Publikováno v:
Journal of Molecular Biology. 291:857-876
The three-dimensional structure of diaminopelargonic acid synthase, a vitamin B6-dependent enzyme in the pathway of the biosynthesis of biotin, has been determined to 1.8 A resolution by X-ray crystallography. The structure was solved by multi-wavele
Autor:
Joseph C. Calabrese, Ayelet Nudelman, Alan R. Rendina, Zdislaw Wawrzak, Dana Marcovici-Mizrahi, George H. Lorimer, Wendy Sue Taylor, Gunter Schneider, Abraham Nudelman, Bruce A. Lockett, W. Huang, Guang Yang, Kevin T. Kranis, Dennis R. Rayner, Barry Arthur Wexler, Ylva Lindqvist, Hongji Chi, Eileen Marsilii, Katharine J. Gibson, Jia Jia
Publikováno v:
Pesticide Science. 55:236-247
Dethiobiotin synthetase (DTBS; E.C. 6.6.6.6), the penultimate enzyme in the biosynthesis of the essential vitamin biotin, is a new potential target for novel herbicides. Inhibitors were designed based on mechanistic and structural information. The in
Publikováno v:
Biochemical and Biophysical Research Communications. 254:632-635
In biotin synthase reactions carried out in vitro, we observed efficient transfer of 35S to biotin from partially purified E. coli biotin synthase (product of the bioB gene) labelled by biosynthetic incorporation of [35S]-cysteine. Mass spectrometry
Autor:
Katharine J. Gibson
Publikováno v:
Biochemistry. 36:8474-8478
Dethiobiotin synthetase (DTBS) catalyzes the formation of the cyclic urea, dethiobiotin (DTB), from (7R,8S)-diaminononanoic acid (DAPA), CO2, and ATP; the other products of the reaction are ADP and Pi. The first intermediate in the reaction sequence
Autor:
Ylva Lindqvist, Günter Schneider, Jia Jia, Weijun Huang, Katharine J. Gibson, Wendy Sue Taylor, Alan R. Rendina
Publikováno v:
Biochemistry. 34:10985-10995
The crystal structures of six complexes of homodimeric Escherichia coli dethiobiotin synthetase with a variety of substrates, substrate analogs, and products have been determined to high resolution. These include (1) the binary complex of dethiobioti
Autor:
Katharine J. Gibson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1169:231-235
Palmitoyl (hexadecanoyl)-acyl carrier protein (ACP) was found to be an alternate substrate for recombinant soybean stearoyl (octadecanoyl)-ACP Δ9-clesaturase. The fatty acid product was identified as palmitoleic acid ((Z)-hexadec-9-enoic acid), whic
Autor:
Katharine J. Gibson, James A. Romesser, Mark Emptage, Patricia J. Litle, Daniel P. O'Keefe, Reijer Lenstra, Charles A. Omer
Publikováno v:
Biochemistry. 30:447-455
We have purified and characterized two ferredoxins, designated Fd-1 and Fd-2, from the soluble protein fraction of sulfonylurea herbicide induced Streptomyces griseolus. These cells have previously been shown to contain two inducible cytochromes P-45
Publikováno v:
Scopus-Elsevier
Recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli, a pyridoxal-phosphate-dependent aminotransferase, has been crystallized in space groups P21 and C2. Both crystal forms were obtained at pH 7.3 with 21% polyethylene glycol and 10%