EC Number   |
|---|
   1.8.1.5 | enzyme free or bound to substrate 2-ketopropyl-CoM, X-ray structure determination and analysis at 1.6-3.5 A resolution, multiple isomorphous replacement and anomalous scattering using four weak heavy atom derivatives |
| 1.8.1.5 | hanging drop vapour diffusion method |
| 1.8.1.5 | in complex with acetoacetate and 2-mercaptoethanesulfonate. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group |
| 1.8.1.5 | vapor diffusion method, using 0.17 M ammonium acetate, 0.085 M trisodium citrate, pH 5.6, 27% (w/v) PEG 4000, and 15% (v/v) glycerol |
