D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase.

Bernard, N.;Johnsen, K;Holbrook, J J;Delcour, Jean
(1995) Biochemical and Biophysical Research Communications — Vol. 208, n° 3, p. 895-900 (1995)

Files

pdfdocument.pdf
  • Restricted Access
  • Adobe PDF
  • 326.51 KB
Request a copy

Details

Authors
  • Bernard, N.
    Author
  • Johnsen, K
    Author
  • Holbrook, J J
    Author
  • Delcour, JeanUCLouvain
    Author
Abstract
The NAD-dependent D-(-)-lactate dehydrogenase (D-LDH) from Lactobacillus delbrueckii subsp. bulgaricus (in short, L. bulgaricus) has been modified at position 175 by site-directed mutagenesis, changing a conserved aspartate residue into an alanine. The D175A mutant enzyme displays a 40-fold shift in coenzyme preference from NADH to NADPH. This demonstrates that D175 truly belongs to the amino acid consensus GXGXXGX(17)D (where X represents any residue) which is the signature of the coenzyme binding site of most NAD-dependent dehydrogenases.
Affiliations

Citations

  • APA
  • Chicago
  • FWB

Bernard, N., Johnsen, K., Holbrook, J. J., & Delcour, J. (1995). D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase. Biochemical and Biophysical Research Communications, 208(3), 895-900. https://doi.org/10.1006/bbrc.1995.1419 (Original work published 1995)