Structural Mechanism of S-Adenosyl Methionine Binding to Catechol O-Methyltransferase
2011

Understanding How SAM Binds to COMT

publication Evidence: moderate

Author Information

Author(s): Tsao Douglas, Diatchenko Luda, Dokholyan Nikolay V.

Primary Institution: University of North Carolina, Chapel Hill

Hypothesis

The metal cation reorients SAM in a conformation suitable for donating its methyl substituent to the recipient ligand.

Conclusion

The study reveals that COMT binds SAM through an induced-fit mechanism, which is influenced by the presence of a divalent metal cation.

Supporting Evidence

  • COMT binds SAM via an induced-fit mechanism.
  • The presence of a divalent metal cation is critical for aligning SAM for catalysis.
  • Docking simulations showed that SAM adopts different poses in the absence and presence of metal.

Takeaway

COMT, an enzyme, needs a special helper called a metal to grab onto another helper called SAM properly, so it can do its job of adding a tiny piece to other molecules.

Methodology

The study used discrete molecular dynamics and computational docking simulations to explore the binding of SAM to COMT.

Limitations

The results are based on computational models and require experimental validation through crystallization of COMT with SAM and metal.

Digital Object Identifier (DOI)

10.1371/journal.pone.0024287

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