EC Number   |
|---|
    4.2.1.17 | at 2.8 A resolution, multidomain protein having 5 domains: A, B, C, D, and E. The N-terminal part has a crotonase fold, which builds the active site for the DELTA3,DELTA2-enoyl-CoA isomerase (EC 5.3.3.8) and DELTA2-enoyl-CoA hydratase-1 |
| 4.2.1.17 | hanging drop method, crystal structure of the enzyme complexed with the potent inhibitor acetoacetyl-CoA, refined at 2.5 A resolution. The active site architecture confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction |
| 4.2.1.17 | hanging drop method, structure of the mitochondrial enoyl-CoA hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A |
| 4.2.1.17 | purified recombinant His-tagged wild-type and SeMet-labeled AtMFP2, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution |
| 4.2.1.17 | structure of enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, refined at a resolution of 2.4 A |
