Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion.

@article{Bahnson2002StructuralMO,
  title={Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion.},
  author={Brian J. Bahnson and Vernon E. Anderson and Gregory A. Petsko},
  journal={Biochemistry},
  year={2002},
  volume={41 8},
  pages={2621-9}
}
We have determined the crystal structure of the enzyme enoyl-CoA hydratase (ECH) from rat liver with the bound substrate 4-(N,N-dimethylamino)cinnamoyl-CoA using X-ray diffraction data to a resolution of 2.3 A. In addition to the thiolester substrate, the catalytic water, which is added in the hydration reaction, has been modeled into well-defined electron density in each of the six active sites of the physiological hexamer within the crystallographic asymmetric unit. The catalytic water… CONTINUE READING

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X-PLOR Version 3.1. A system for X-ray Crystallography and NMR

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