Substrate and product specificity of Arthrobacter sialophilus neuraminidase.
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منابع مشابه
Substrate and product specificity of Arthrobacter sialophilus neuraminidase.
Arthrobacter sialophilus neuraminidase catalyzes the hydrolysis of N-acetylneuraminyl-alpha-oxygen, nitrogen, and azido glycosides. The most effective of those substrates examined was N-acetylneuraminyl-alpha-4-methylumbelliferylglycoside (AcNeu-alpha-4-MU; Km app, 0.0193 mM; kcat, 136.4 sec-1). The products resulting from the enzymic hydrolysis of N-acetylneuraminyl-alpha-azido-glycoside were ...
متن کاملStructural requirements for neuraminidase induction in Arthrobacter sialophilus.
The effectiveness of 13 N-acetylneuraminic acid derivatives as potential inducers of Arthrobacter sialophilus neuraminidase were examined. N-Acetylneuraminic acid nitrogen and thioglycosides were not inducers, whereas 2,3-dehydro-N-acetylneuraminic acid, a transition state analog for neuraminidases, was the most effective inductive ligand. The C-4 hydroxyl function of N-acetylneuraminic acid wa...
متن کاملFluorescent assay for studying the substrate specificity of neuraminidase.
Toyopearl 650 M was purchased from Tosoh (Japan). The 10-~1 pipette tips with filter (cat. no. FI08-96R-I0) and thin-well 0.2-ml PCR microtubes (cat. no. 430-01XNBZ-Q) with caps were obtained from Porex. Black polystyrene 96-well microtiter plates were purchased from Nunc (Denmark, cat. no. 437111). Vibrio cholerae neuraminidase (3.2.1.18) was purchased from Sigma (USA). 3'SiaLac and 6'SiaLac w...
متن کاملProperties of an inducible extracellular neuraminidase from an Arthrobacter isolate.
The elective isolation of a soil microorganism, tentatively assigned to the genus Arthrobacter, which produced an extracellular neuraminidase is described. The secretion of neuraminidase from washed cells in minimal medium required the presence of sialo-containing glycoproteins, whereas free N-acetyl-neuraminic asid of N-acetylmannosamine were poor inducers. No enzyme could be dected in the ind...
متن کاملApplications of a synthetic neuraminidase substrate.
A rapid and precise assay for neuraminidase using 2-(3'-methoxyphenyl)-N-acetyl-alpha-neuraminic acid (MPN) is described. It is proposed that this substrate be used for the standardization of activity of neuraminidases from viral, bacterial, and mammalian sources. MPN is also used as a chromogenic substrate to localize influenza and parainfluenza virus foci in tissue culture. This technique per...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34634-9