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Membrane-bound diiron proteins

Fatty acyl-CoA desaturases are terminal oxidases of a membrane-bound enzyme complex that also includes cytochrome b5 and cytochrome b5 reductase (Bloomfield and Bloch, 1960). They remove substrate hydrogen atoms at a position determined by the specificity of the enzyme. They play essential roles in regulating membrane fluidity and are also involved in insect lipid and pheromone metabolism. They share the presence of three highly conserved histidine-rich sequences (H-boxes) that coordinate the diiron-oxo structure at the active sites (Shanklin and Cahoon, 1998) and four hydrophobic a helices that appear to anchor the protein into the lipid bilayer and situate the H-boxes in their correct position in the active site. [Pg.54]


See other pages where Membrane-bound diiron proteins is mentioned: [Pg.273]    [Pg.273]    [Pg.353]    [Pg.478]    [Pg.2237]    [Pg.493]    [Pg.494]    [Pg.399]    [Pg.254]    [Pg.2236]    [Pg.321]    [Pg.275]    [Pg.316]    [Pg.18]   
See also in sourсe #XX -- [ Pg.353 , Pg.355 ]




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