Revealing coupling patterns in isoprenoid alkylation biocatalysis.
Diversity of scaffold structure and function is a hallmark of the >50,000 isoprenoid natural products such as taxol. Whereas most members of this class are assembled by iterative head-to-tail enzymatic joining reactions between delta2- and delta3-isopentenyl diphosphate (IPP) monomers, dimerization of two delta2-IPP molecules has now been shown to account for three additional modes of "irregular" coupling patterns at the level of C10 monoterpene scaffolds.
Walsh
Christopher T
CT
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA. christopher_walsh@hms.harvard.edu
D000478:Alkylation; D002384:Catalysis; D019281:Dimerization; D051231:Farnesyltranstransferase / Q000737:chemistry; D051228:Geranyltranstransferase / Q000737:chemistry; D045782:Hemiterpenes / Q000737:chemistry*; D007536:Isomerism; D015394:Molecular Structure; D009943:Organophosphorus Compounds / Q000737:chemistry*; D013729:Terpenes / Q000138:chemical synthesis* / Q000737:chemistry
D045782:Hemiterpenes; D009943:Organophosphorus Compounds; D013729:Terpenes; C004809:isopentenyl pyrophosphate; C043060:3,3-dimethylallyl pyrophosphate; C518835:chrysanthemyl diphosphate synthase, Chrysanthemum; D051228:Geranyltranstransferase; D051231:Farnesyltranstransferase