Mechanism of radical-based catalysis in the reaction catalyzed by adenosylcobalamin-dependent ornithine 4,5-aminomutase.

@article{Wolthers2008MechanismOR,
  title={Mechanism of radical-based catalysis in the reaction catalyzed by adenosylcobalamin-dependent ornithine 4,5-aminomutase.},
  author={Kirsten Wolthers and Stephen E J Rigby and Nigel S. Scrutton},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 50},
  pages={
          34615-25
        }
}
We report an analysis of the reaction mechanism of ornithine 4,5-aminomutase, an adenosylcobalamin (AdoCbl)- and pyridoxal L-phosphate (PLP)-dependent enzyme that catalyzes the 1,2-rearrangement of the terminal amino group of D-ornithine to generate (2R,4S)-2,4-diaminopentanoic acid. We show by stopped-flow absorbance studies that binding of the substrate D-ornithine or the substrate analogue D-2,4-diaminobutryic acid (DAB) induces rapid homolysis of the AdoCbl Co-C bond (781 s(-1), D-ornithine… CONTINUE READING

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Mechanism of Ornithine 4,5-Aminomutase 34624 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • V. Bandarian, G. H. Reed
  • U G I SE R V E I D A D Q U ISIC IO N S on M arch…
  • 2008
1 Excerpt

ISIC IO N S on M arch 4, 2015 hp://w w w .jb.org/ D ow nladed from Nigel

  • R. G. Finke, B. P. Hay
  • Inorg. Chem
  • 1984
1 Excerpt