Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release.

@article{Hunter1999PresteadystateRO,
  title={Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release.},
  author={Gregory A. Hunter and Gloria C. Ferreira},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 18},
  pages={12222-8}
}
5-Aminolevulinate synthase (ALAS) is the first enzyme of the heme biosynthetic pathway in non-plant eukaryotes and the alpha-subclass of purple bacteria. The pyridoxal 5'-phosphate cofactor at the active site undergoes changes in absorptive properties during substrate binding and catalysis that have allowed us to study the kinetics of these reactions spectroscopically. Rapid scanning stopped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction with glycine… CONTINUE READING