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 language | English |
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Pages (from-to) | 2455-2459 |
Number of pages | 5 |
Journal | ChemBioChem |
Volume | 10 |
Issue number | 15 |
Early online date | 8 Sept 2009 |
DOIs | |
Publication status | Published - 12 Oct 2009 |
Bibliographical note
Funding InformationBBSRC. Grant Number: BB/F007426/1 and BBS/B/14426
NIH. Grant Number: CA127622
Scottish Funding Council
Keywords
- biosynthesis
- catalysis
- enzyme catalysis
- enzymes