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...
Hauptverfasser: | Lohans, C, Wang, D, Wang, J, Hamed, R, Schofield, C |
---|---|
Format: | Journal article |
Veröffentlicht: |
American Chemical Society
2017
|
Ähnliche Einträge
Ähnliche Einträge
-
Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity.
von: Hamed, R, et al.
Veröffentlicht: (2008) -
Use of methylmalonyl‐CoA epimerase in enhancing crotonase stereoselectivity
von: Hamed, R, et al.
Veröffentlicht: (2015) -
Crotonase catalysis enables flexible production of functionalized prolines and carbapenams.
von: Hamed, R, et al.
Veröffentlicht: (2012) -
Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily.
von: Batchelar, E, et al.
Veröffentlicht: (2008) -
Biocatalytic production of bicyclic β-lactams with three contiguous chiral centres using engineered crotonases
von: Hamed, R, et al.
Veröffentlicht: (2019)