Structure-function relationships in lactate dehydrogenase.

@article{Adams1973StructurefunctionRI,
  title={Structure-function relationships in lactate dehydrogenase.},
  author={Margaret J Adams and Manfred Buehner and K P Chandrasekhar and Geoffrey Ford and Marvin L. Hackert and Anders Liljas and Michael G. Rossmann and I E Smiley and William S. Allison and Johannes Everse and Nathan O. Kaplan and Susan S. Taylor},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1973},
  volume={70 7},
  pages={1968-72}
}
The binding of coenzyme and substrate are considered in relation to the known primary and tertiary structure of lactate dehydrogenase (EC 1.1.1.27). The adenine binds in a hydrophobic crevice, and the two coenzyme phosphates are oriented by interactions with the protein. The positively charged guanidinium group of arginine 101 then folds over the negatively charged phosphates, collapsing the loop region over the active center and positioning the unreactive B side of the nicotinamide in a… CONTINUE READING
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