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Yeast hexokinase glucose site

The x-ray structure for yeast hexokinase is also available. Thus, glucose analogs are now being used to elucidate minute details of the catalytic mechanism. Recently D- lose was used in crystallographic work to show that the 6-hydro ethyl group of the natural substrate is necessary for substrate-induced closure of the active-site cleft (81 ). This induced closure, which is observed with glucose binding (82), is believed to be a part of the induced fit mechanism postulated for hexokinase (83) ... [Pg.200]

See other pages where Yeast hexokinase glucose site is mentioned: [Pg.362]    [Pg.656]    [Pg.74]    [Pg.119]    [Pg.171]    [Pg.111]    [Pg.339]    [Pg.223]    [Pg.1116]   
See also in sourсe #XX -- [ Pg.28 ]

See also in sourсe #XX -- [ Pg.348 , Pg.349 ]



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