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