Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62)

Hai Deng, Stephen A McMahon, Alessandra S Eustaquio, Bradley S Moore, James H Naismith, David O'Hagan

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Abstract

The substrate analogue S-adenosyl-l-homocysteine (SAH) was co-crystallised with SAM hydroxide adenosyltransferase from Pyrococcus horikoshii. Of the two active site water molecules one appears to be structural and the other is a candidate for nucleophilic attack, to become the C5′ adenosyl hydroxyl group. The data support a mechanism in which the Arg–Asp ion pair is important for positioning both water molecules.
Original languageEnglish
Pages (from-to)2455-2459
Number of pages5
JournalChemBioChem
Volume10
Issue number15
Early online date8 Sep 2009
DOIs
Publication statusPublished - 12 Oct 2009

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Keywords

  • biosynthesis
  • catalysis
  • enzyme catalysis
  • enzymes

Cite this

Deng, H., McMahon, S. A., Eustaquio, A. S., Moore, B. S., Naismith, J. H., & O'Hagan, D. (2009). Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62). ChemBioChem, 10(15), 2455-2459. https://doi.org/10.1002/cbic.200900369