Evolving biosynthetic tangos negotiate mechanistic landscapes.
The dependence of polyketide synthase and terpene cyclase mechanistic adaptation on the chemistry of their oligomeric substrates illuminates a convergent evolutionary strategy for shaping cyclization in these otherwise disparate reactions. Evolution of these enzyme families relies on rhythmic tangos, in which the enzymes and substrates together determine product outcome by negotiating decision networks governing intrinsic and induced chemical reactivities.
Austin
Michael B
MB
The Salk Institute for Biological Studies, Jack H. Skirball Center for Chemical Biology and Proteomics, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
O'Maille
Paul E
PE
Noel
Joseph P
JP
D001665:Binding Sites; D019755:Carbon-Carbon Lyases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D002384:Catalysis; D019143:Evolution, Molecular; D018942:Macrolides / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D048630:Polyketide Synthases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D018942:Macrolides; D048630:Polyketide Synthases; D019755:Carbon-Carbon Lyases; C051130:trichodiene synthetase