Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: structural mechanism.

@article{MoosaviMovahedi2013ThermalIA,
  title={Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: structural mechanism.},
  author={Faezeh Moosavi-Movahedi and Ali Akbar Saboury and Hamid Hadi Alijanvand and M. Saeed Bohlooli and Maryam Sadat Salami and Ali Akbar Moosavi-Movahedi},
  journal={International journal of biological macromolecules},
  year={2013},
  volume={58},
  pages={66-72}
}
Horse liver alcohol dehydrogenase (HLADH) is a two subunits metal enzyme that has two catalytic sites and two coenzyme domains for each subunit. These subunits are connected together by coenzyme domains. In this study, we investigated the number and sequences of residues that participated in interface locks of HLADH. For this purpose, the kinetics of… CONTINUE READING