Crotonases: Nature’s exceedingly convertible catalysts
The crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Many crotonases employ oxyanion holemediated stabilization of intermediates to catalyze the reaction of coenzyme A (CoA) thioester substrates (e.g., malonyl-CoA, a,β- uns...
Main Authors: | Lohans, C, Wang, D, Wang, J, Hamed, R, Schofield, C |
---|---|
Format: | Journal article |
Udgivet: |
American Chemical Society
2017
|
Lignende værker
-
Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity.
af: Hamed, R, et al.
Udgivet: (2008) -
Use of methylmalonyl‐CoA epimerase in enhancing crotonase stereoselectivity
af: Hamed, R, et al.
Udgivet: (2015) -
Crotonase catalysis enables flexible production of functionalized prolines and carbapenams.
af: Hamed, R, et al.
Udgivet: (2012) -
Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily.
af: Batchelar, E, et al.
Udgivet: (2008) -
Biocatalytic production of bicyclic β-lactams with three contiguous chiral centres using engineered crotonases
af: Hamed, R, et al.
Udgivet: (2019)