Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.

@article{Thom1998StabilizationOR,
  title={Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.},
  author={Nicolas H Thom{\"a} and Thorsten Meier and Philip Rainsford Evans and Peter Francis Leadlay},
  journal={Biochemistry},
  year={1998},
  volume={37 41},
  pages={
          14386-93
        }
}
The adenosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the reversible rearrangement of methylmalonyl-CoA into succinyl-CoA by a free-radical mechanism. The recently solved X-ray crystal structure of methylmalonyl-CoA mutase from Propionibacterium shermanii has shown that tyrosine 89 is an active-site residue involved in substrate binding. The role of tyrosine 89, a conserved residue among methylmalonyl-CoA mutases, has been investigated by using site-directed mutagenesis to replace… CONTINUE READING
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