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Enzyme, cleft control

The cleft size of phosphotransferases might be on the order of a diameter of 10 A. However, it should be recognized that the size is varied under the influence of controlling ligands such as observed in allosteric enzymes. [Pg.170]

How do these cyclase enzymes control the precise regiochem-istry and stereochemistry of these multistep cyclizations The active site of pentalenene synthase consists of a hydrophobic cleft, which is lined with aromatic and nonpolar residues. It is thought that the carbocation intermediates might be stabilized by the formation of tt-cation interactions, with aromatic residues such as phenylalanine, tyrosine, and tryptophan. In pentalenene synthase, replacement of Phe-76 or Phe-77 by Ala gave > 10-fold reduction in activity, which suggests that they may stabilize carbocationic intermediates through Jt-cation interactions. [Pg.432]

See other pages where Enzyme, cleft control is mentioned: [Pg.72]    [Pg.28]    [Pg.1279]    [Pg.36]    [Pg.80]    [Pg.9]    [Pg.132]    [Pg.550]    [Pg.641]    [Pg.38]    [Pg.701]    [Pg.33]    [Pg.520]    [Pg.161]    [Pg.109]    [Pg.113]    [Pg.253]    [Pg.278]    [Pg.137]    [Pg.201]    [Pg.206]    [Pg.28]    [Pg.1279]    [Pg.144]    [Pg.111]    [Pg.350]    [Pg.110]    [Pg.230]    [Pg.1100]    [Pg.75]    [Pg.79]    [Pg.284]    [Pg.394]    [Pg.145]    [Pg.426]    [Pg.161]    [Pg.54]    [Pg.183]    [Pg.2711]    [Pg.42]    [Pg.258]    [Pg.26]    [Pg.207]    [Pg.236]   
See also in sourсe #XX -- [ Pg.177 , Pg.190 , Pg.191 , Pg.206 , Pg.207 , Pg.208 , Pg.216 ]



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