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Yeast a-glucosidase

Because sucrose is hydrolyzed by enzymes that specifically assist hydrolysis of both a glycosides (such as yeast a-glucosidase) and /3-fructosides (such as invertase), it is inferred that the glucose residue is present as an a glucoside and the fructose residue as a /3 fructoside. If so, the remaining uncertainty in the structure of sucrose is the size of the rings in the glucose and fructose residues. [Pg.930]

An analogous mechanism that relies on proton transfer and nucleophilic attack is apparently operative with aziridine derivatives of conduritol and deoxynojirimycin. Preliminary studies show both compounds are effective inhibitors the conduritol B aziridine (X) irreversibly inactivates Alcaligenesfaecalis )3-glucosidase and yeast a-glucosidase (2i8),and the ga/ac/odeoxynojirimycin aziridine (XI)... [Pg.216]

Dideoxy-1,4-imino-D-arabiiutol 2R, >RAR)-2-hydroxymethyl pyrrolidine-3,4-diol, DABl, 1] has been found in ho h Arachniodes standishii andAngylocalyx boutiqueanus and it is a potent inhibitor of yeast a-glucosidase (50% inhibition at 1.8 x 10 ... [Pg.1]

Bacillus cereus, against, 64 bacterial infections, 240 bacterial lipopolysaccharides, 1 Baker s yeast a-glucosidase inhibitor, 11 biochemistry and pathology in big, 320 biological, 1,75, 105, 193, 209, 212,... [Pg.429]

In the yeast a-glucosidase-catalyzed hydrolysis of 4-nitrophenyl-a-D-glucopyr-anoside," the primary leaving group KIE was unity, 1.001, and the a-secondary... [Pg.261]

KIEs on Emax were investigated for the yeast a-glucosidase-catalyzed hydrolysis of... [Pg.286]

The )8-secondary KIEs for yeast a-glucosidase-catalyzed hydrolysis of 10 and 11 are suggestive of substantial overlap of a C-H(D) bond with the p-orbital at the transition state, consistent with the glycosyl ring approaching a boat conformation. Hosie and Sinnott had reported a similar value for the )8-secondary HKIE on 10 as well as a large value for 12." ... [Pg.286]

The primary KIEs for the spontaneous hydrolysis of 12 (1.018, corrected to 25°C) and the yeast a-glucosidase-catalyzed hydrolysis of 10 (1.019) suggested transition states with partial C-N bond cleavage. Similar results were found in a study by Scheming and Schramm on pertussis toxin-catalyzed hydrolysis of NAD. ° Based on the family of KIEs (primary KIE value of 1.021), semi-empirical calculations and BOVA, these authors concluded that the reaction transition state had partial C-N bond breakage with a weak nucleophilic component from the incoming water molecule. [Pg.288]


See other pages where Yeast a-glucosidase is mentioned: [Pg.59]    [Pg.525]    [Pg.526]    [Pg.366]    [Pg.143]    [Pg.183]    [Pg.98]    [Pg.407]    [Pg.1893]    [Pg.2011]    [Pg.2090]    [Pg.2097]    [Pg.354]    [Pg.131]    [Pg.392]    [Pg.316]    [Pg.338]    [Pg.384]    [Pg.385]    [Pg.394]    [Pg.79]    [Pg.79]    [Pg.1379]    [Pg.217]    [Pg.217]    [Pg.11]    [Pg.237]    [Pg.285]    [Pg.286]    [Pg.288]    [Pg.395]    [Pg.395]    [Pg.178]   
See also in sourсe #XX -- [ Pg.98 ]




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