Publications by authors named "E A Wenger"
Crystal structure of di-μ-acetato-κ :-bis{(acetato-κ ,')tetra-aqua-[1-(pyridin-2-yl-methylidene-κ)-2-(pyridin-2-yl-κ)hydrazine-κ ]lanthanum(III)} dinitrate hemihydrate.
Acta Crystallogr E Crystallogr Commun
January 2025
In the binuclear title complex, [La(CHO)(CHN)(HO)](NO)·0.5HO, the two lanthanum ions are nine coordinate in a distorted trigonal-prismatic geometry. Each La ion is bonded to three N atoms of the Schiff base, 1-(pyridin-2-yl)-2-(pyridin-2-yl-methyl-ene)hydrazine and is coordinated by one acetate group, which acts in -bidentate mode and two acetate groups that act in -mode between the two La ions.
View Article and Find Full Text PDFAn unusual family of bifunctional terpene synthases has been discovered in which both catalytic domains - a prenyltransferase and a cyclase - are connected by a long, flexible linker. These enzymes are unique to fungi and catalyze the first committed steps in the biosynthesis of complex terpenoid natural products: the prenyltransferase assembles 5-carbon precursors to form C geranylgeranyl diphosphate (GGPP), and the cyclase converts GGPP into a polycyclic hydrocarbon product. Weak domain-domain interactions as well as linker flexibility render these enzymes refractory to crystallization and challenge their visualization by cryo-EM.
View Article and Find Full Text PDFEngineering substrate channeling in a bifunctional terpene synthase.
Proc Natl Acad Sci U S A
October 2024
Article Synopsis
- Fusicoccadiene synthase (PaFS) is a complex enzyme with two main functions: it synthesizes geranylgeranyl diphosphate (GGPP) from smaller molecules and then converts GGPP into fusicoccadiene, a key precursor for another compound.
- The enzyme's two functional domains (prenyltransferase and cyclase) are connected by a flexible linker, allowing the cyclase domains to randomly interact with the central prenyltransferase core, facilitating efficient substrate channeling.
- Research shows that even without a covalent bond between the domains, the cyclase can effectively channel GGPP for conversion, suggesting that physical proximity and structural flexibility play crucial roles in the enzyme's efficiency.
Article Synopsis
- - Hyoscyamine 6β-hydroxylase (H6H) is an enzyme that uses iron and 2-oxoglutarate to convert hyoscyamine into the antinausea drug scopolamine through a two-step process involving hydroxylation and epoxidation.
- - The enzyme first performs hydroxylation at the C6 position before coupling it to the C7 position, but the mechanism of how H6H prefers this route over simply hydroxylating at C7 is unclear.
- - Research shows that H6H does not rely on substrate positioning for epoxidation; instead, a small angle change in how the iron approaches the substrate influences whether it performs hydroxylation