Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.

@article{Razeto2002DomainCS,
  title={Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.},
  author={Adelia Razeto and Sunil Kochhar and Herbert Hottinger and Miroslava Dauter and Keith S Wilson and Victor S. Lamzin},
  journal={Journal of molecular biology},
  year={2002},
  volume={318 1},
  pages={109-19}
}
NAD-dependent Lactobacillus bulgaricus D-Lactate dehydrogenase (D-LDHb) catalyses the reversible conversion of pyruvate into D-lactate. Crystals of D-LDHb complexed with NADH were grown and X-ray data collected to 2.2 A. The structure of D-LDHb was solved by molecular replacement using the dimeric Lactobacillus helveticus D-LDH as a model and was refined to an R-factor of 20.7%. The two subunits of the enzyme display strong asymmetry due to different crystal environments. The opening angles of… CONTINUE READING

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