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Threonine residues cytochrome

After activation, protein kinase C phosphorylates specific serine and threonine residues in target proteins. As with cAMP-stimulated protein kinase, the specific cellular responses to protein kinase C activation depend on the ensemble of target proteins that become phosphorylated in a given cell. Known target proteins include calmodulin, the insulin receptor, / -adrenergic receptor, glucose transporter, HMG-CoA reductase, cytochrome P-450, and tyrosine hydroxylase. [Pg.1279]

Site-directed mutagenesis studies on cytochromes P450 have revealed the importance of active site amino acid residues. In sMMO, an active site cysteine and threonine may have important mechanistic consequences. Although the significance of these residues is not yet known, it may be necessary to consider their roles when... [Pg.318]


See other pages where Threonine residues cytochrome is mentioned: [Pg.411]    [Pg.188]    [Pg.41]    [Pg.473]    [Pg.574]    [Pg.311]    [Pg.2357]    [Pg.166]    [Pg.350]    [Pg.348]    [Pg.427]    [Pg.348]    [Pg.410]    [Pg.103]    [Pg.162]    [Pg.309]    [Pg.93]    [Pg.94]    [Pg.1660]   
See also in sourсe #XX -- [ Pg.410 , Pg.423 , Pg.461 ]




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