Mechanism for folate-independent aldolase reaction catalyzed by serine hydroxymethyltransferase
Article first published online: 23 DEC 2011
© 2011 The Authors Journal compilation © 2011 FEBS
Volume 279, Issue 3, pages 504–514, February 2012
How to Cite
Chiba, Y., Terada, T., Kameya, M., Shimizu, K., Arai, H., Ishii, M. and Igarashi, Y. (2012), Mechanism for folate-independent aldolase reaction catalyzed by serine hydroxymethyltransferase. FEBS Journal, 279: 504–514. doi: 10.1111/j.1742-4658.2011.08443.x
- Issue published online: 18 JAN 2012
- Article first published online: 23 DEC 2011
- Accepted manuscript online: 5 DEC 2011 11:50AM EST
- (Received 24 September 2011, revised 15 November 2011, accepted 29 November 2011)
Fig. S1. Multiple-sequence alignment of SHMTs from bacteria and archaea obtained using clustalw program on UniProt server. Asterisks denote identical residues. Colons and periods correspond to highly and weakly conserved residues. White letters on black ground and dark-shaded letters indicate amino acids expected to form hydrogen bonds and hydrophobic interactions with l-allo-threonine–PLP aldimine, respectively, based on sequence similarity with bsSHMT, whose crystal structure is determined in complex with l-allo-threonine.
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