Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.

@article{Coll1990EnzymaticMO,
  title={Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.},
  author={M. Dolores Coll and S H Knof and Yoshimi Ohga and Albrecht Messerschmidt and Robert Huber and Harold Moellering and Lorenz R{\"u}ssmann and G{\"u}nter Schumacher},
  journal={Journal of molecular biology},
  year={1990},
  volume={214 2},
  pages={597-610}
}
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the… CONTINUE READING

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