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Enzymes Active sites, detailed chemical nature

Cyclization of an allylic pyrophosphate is a key step in the biosynthesis of most monoterpenes. Early hypotheses concerning the nature of the acyclic precursor and the cyclization process are first described, and chemical models for the cyclization presented. Following a review of several representative cyclase enzymes and the reactions that they catalyze, a series of stereochemical and mechanistic experiments with partially purified cyclases are reported. The results of these studies have allowed a detailed description of events at the active site and the formulation of a unified stereochemical scheme for the multistep isomerization-cyclization reaction by which the universal precursor geranyl pyrophosphate is transformed to cyclic monoterpenes. [Pg.134]


See other pages where Enzymes Active sites, detailed chemical nature is mentioned: [Pg.6]    [Pg.92]    [Pg.123]    [Pg.38]    [Pg.53]    [Pg.272]    [Pg.2117]    [Pg.272]    [Pg.630]    [Pg.244]    [Pg.576]    [Pg.633]    [Pg.974]    [Pg.973]    [Pg.59]    [Pg.199]    [Pg.1495]    [Pg.458]    [Pg.13]    [Pg.249]    [Pg.1334]    [Pg.98]    [Pg.527]    [Pg.405]    [Pg.3173]    [Pg.3]    [Pg.327]    [Pg.310]   
See also in sourсe #XX -- [ Pg.290 , Pg.291 ]




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Active sites, nature

Chemical activity

Chemical nature

Chemically active

Chemicals sites

Enzyme natural

Enzymes activator sites

Enzymes active sites

Enzymes active sites, nature

Enzymes nature

Natural chemicals

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