Structural highlights
Function
[PENA_STREX] Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.,Lesburg CA, Zhai G, Cane DE, Christianson DW Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cane DE, Sohng JK, Lamberson CR, Rudnicki SM, Wu Z, Lloyd MD, Oliver JS, Hubbard BR. Pentalenene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319. Biochemistry. 1994 May 17;33(19):5846-57. PMID:8180213
- ↑ Lesburg CA, Zhai G, Cane DE, Christianson DW. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology. Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272
