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

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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
Issue number15
Early online date8 Sept 2009
Publication statusPublished - 12 Oct 2009

Bibliographical note

Funding Information
BBSRC. Grant Number: BB/F007426/1 and BBS/B/14426
NIH. Grant Number: CA127622
Scottish Funding Council


  • biosynthesis
  • catalysis
  • enzyme catalysis
  • enzymes


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