Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases.

ABSTRACT: Terpene synthases are a mechanistically intriguing family of enzymes that catalyze complex, multistep reactions that are capable of generating hundreds of structurally diverse hydrocarbon and oxygenated scaffolds of biological and commercial importance. Interestingly, distantly related terpene synthases from fungi to plants all contain an invariant three-dimensional fold, and molecular comparisons of their active sites indicate that they are enriched with relatively inert amino acid residues that do not react directly with the reaction intermediates. Therefore, catalytic specificity appears to rely on the contour and dynamics of the active site created by the positioning of amino acid backbones and side chains on this catalytic surface and by supporting layers of residues surrounding the s

SUBMITTER: Greenhagen BT 

PROVIDER: S-EPMC1502538 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature