Trehalose Mediated Inhibition of Lactate Dehydrogenase from Rabbit Muscle. The Application of Kramers' Theory in Enzyme Catalysis.

J. M. Hernández-Meza; J. Sampedro

DOI:10.1021/acs.jpcb.8b01656

Corpus ID: 4976153

Trehalose Mediated Inhibition of Lactate Dehydrogenase from Rabbit Muscle. The Application of Kramers' Theory in Enzyme Catalysis.

@article{HernndezMeza2018TrehaloseMI,
  title={Trehalose Mediated Inhibition of Lactate Dehydrogenase from Rabbit Muscle. The Application of Kramers' Theory in Enzyme Catalysis.},
  author={J. M. Hern{\'a}ndez-Meza and J. Sampedro},
  journal={The journal of physical chemistry. B},
  year={2018},
  volume={122 15},
  pages={
          4309-4317
        }
}

J. M. Hernández-Meza, J. Sampedro

Published 2018

Chemistry, Medicine

The journal of physical chemistry. B

Lactate dehydrogenase (LDH) catalyzes the reduction of pyruvate to lactate by using NADH. LDH kinetics has been proposed to be dependent on the dynamics of a loop over the active site. Kramers' theory has been useful in the study of enzyme catalysis dependent on large structural dynamics. In this work, LDH kinetics was studied in the presence of trehalose and at different temperatures. In the absence of trehalose, temperature increase raised exponentially the LDH Vmax and revealed a sigmoid… CONTINUE READING

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