Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.

@article{Cobessi2000StructuralAB,
  title={Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.},
  author={David Cobessi and Fr{\'e}d{\'e}rique T{\^e}te-Favier and St{\'e}phane Marchal and Guy Branlant and Andr{\'e} Aubry},
  journal={Journal of molecular biology},
  year={2000},
  volume={300 1},
  pages={141-52}
}
The NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (abbreviated Sm-ALDH) belongs to the aldehyde dehydrogenase (ALDH) family. Its catalytic mechanism proceeds via two steps, acylation and deacylation. Its high catalytic efficiency at neutral pH implies prerequisites relative to the chemical mechanism. First, the catalytic Cys284 should be accessible and in a thiolate form at physiological pH to attack efficiently the aldehydic group of the… CONTINUE READING

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