Cooperativity in nicotinamide adenine dinucleotide binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase.

@article{Wei2000CooperativityIN,
  title={Cooperativity in nicotinamide adenine dinucleotide binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase.},
  author={Baoxian Wei and Lisheng Ni and Thomas D. Hurley and Henry Weiner},
  journal={Biochemistry},
  year={2000},
  volume={39 18},
  pages={5295-302}
}
The low-activity Oriental variant of human mitochondrial aldehyde dehydrogenase possesses a lysine rather than a glutamate at residue 487 in the 500 amino acid homotetrameric enzyme. The glutamate at position 487 formed two salt bonds, one to an arginine at position 264 in the same subunit and the other to arginine 475 in a different subunit [Steinmetz, C. G., Xie, P.-G.,Weiner, H., and Hurley, T. D. (1997) Structure 5, 2487-2505]. Mutating arginine 264 to glutamine produced a recombinantly… CONTINUE READING
Highly Cited
This paper has 25 citations. REVIEW CITATIONS