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Palmitoleate-bound

Figure 13 The active-site structure of P450bm-3 with palmitoleic acid bound to the substrate pocket. The fatty acid substrate extends along the substrate access channel to the surface of the protein. The side chains lining the channel are also shown... Figure 13 The active-site structure of P450bm-3 with palmitoleic acid bound to the substrate pocket. The fatty acid substrate extends along the substrate access channel to the surface of the protein. The side chains lining the channel are also shown...
Figure 12.1 The crystal structure of the P450BM3 monooxygenase domain with palmitoleic acid bound (adapted from pdb ISMJ) heme and palmitoleic acid in black. Figure 12.1 The crystal structure of the P450BM3 monooxygenase domain with palmitoleic acid bound (adapted from pdb ISMJ) heme and palmitoleic acid in black.
Soluble enzymes are much easier to study, so more is known of the first type, but from many studies with a variety of spectroscopic. X-ray and molecular biological techniques, it seems the mechanism of reaction is the same in both types. Although the full story of the enzymes is not yet known, the description here summarizes our present knowledge of membrane-bound fatty acid desaturases found in insects. The description is of a A9-desaturase, the most common type, which converts stearic acid to oleic acid. The location of the double bond is measured from the carboxylate end of the molecule. Palmitic acid with the same enzyme gives palmitoleic acid. If an unnatural Cjy or C19 acid is supplied to the... [Pg.32]


See other pages where Palmitoleate-bound is mentioned: [Pg.305]    [Pg.310]    [Pg.311]    [Pg.305]    [Pg.310]    [Pg.311]    [Pg.24]    [Pg.333]    [Pg.306]    [Pg.312]    [Pg.81]    [Pg.105]    [Pg.131]    [Pg.13]    [Pg.343]   
See also in sourсe #XX -- [ Pg.3 , Pg.450 ]




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