Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Jacqueline N. Watson"'
Autor:
Matthew C. Deen, Fahimeh S. Shidmoossavee, Saeideh Shamsi Kazem Abadi, Andrew J. Bennet, Jacqueline N. Watson
Publikováno v:
Glycobiology. 30(5)
N-acetylneuraminic acid (5-acetamido-3,5-dideoxy-d-glycero-d-galacto-non-2-ulosonic acid), which is the principal sialic acid family member of the non-2-ulosonic acids and their various derivatives, is often found at the terminal position on the glyc
Autor:
Andrew J. Bennet, Jefferson Y. Chan, Thor J. Borgford, Jacqueline N. Watson, April Lu, Viviana C. Cerda
Publikováno v:
Biochemistry. 51:433-441
Mutagenesis of the conserved glutamic acid of influenza type A (E277) and Micromonospora viridifaciens (E260) sialidases was performed to probe the contribution of this strictly conserved residue to catalysis. Kinetic studies of the E260D and E260C M
Publikováno v:
Glycobiology. 17:401-410
Aspergillus fumigatus is an opportunistic fungal pathogen that causes a life-threatening invasive fungal disease (invasive aspergillosis, IA) in immunocompromised individuals. The first step of pathogenesis is thought to be the attachment of conidia
Publikováno v:
Biochemistry. 45:13264-13275
The Y370G inverting mutant sialidase from Micromonospora viridifaciens possesses beta-sialidase activity with phenyl beta-sialoside (Ph-betaNeuAc) to give alpha-sialic acid as the first formed product. The derived catalytic rate constants for k(cat)
Publikováno v:
Biochemistry. 45:9319-9326
The sialidase from Micromonospora viridifaciens has been found to catalyze the hydrolysis of aryl 2-thio-alpha-D-sialosides with remarkable efficiency: the first- and second-order rate constants, kcat and kcat/Km, for the enzyme-catalyzed hydrolysis
Publikováno v:
Biochemistry. 44:9117-9122
Mutagenesis of the conserved tyrosine (Y370) of the Micromonospora viridifaciens sialidase to small amino acids changes the mechanism of catalysis from retention of anomeric configuration to inversion [Watson, J. N., et al. (2003) Biochemistry 42, 12
Autor:
Doug T. H. Chou, Johnny H Chen, Jacqueline N. Watson, Andrew J. Bennet, Thor J. Borgford, Tara L. Knoll
Publikováno v:
Biochemistry and Cell Biology. 83:115-122
Investigations into subtle changes in the catalytic activity of sialidases have been performed using enzymes from several different origins, and their results have been compared. This work highlights the potential pitfalls encountered when extending
Autor:
Andrew J. Bennet, Doug T. H. Chou, Andrew A. Scholte, Thor J. Borgford,‡ and, Jacqueline N. Watson
Publikováno v:
Journal of the American Chemical Society. 122:8357-8364
A reagent panel, comprised of five pyridinium salts of α-d-N-acetylneuraminic acid, was synthesized and then used to probe enzymatic (α-sialidase) and nonenzymatic mechanisms of neuraminide hydroly...
Publikováno v:
Biochemistry. 49(30)
The Micromonospora viridifaciens Y370G inverting mutant sialidase has been found to possess beta-sialidase activity with various fluoro-substituted phenyl beta-sialosides. A reagent panel of seven mono- and difluorophenyl beta-d-sialosides was synthe
Publikováno v:
Organicbiomolecular chemistry. 4(24)
Two isomeric 4-methylumbelliferyl-alpha-D-N-acetylneuraminylgalactopyranosides (1 and 2) were synthesised. These compounds contain either the natural alpha-2,3 or alpha-2,6 sialyl-galactosyl linkages, as well as an attached 4-methylumbelliferone for