Identification of an essential active-site residue in the α-d-phosphohexomutase enzyme superfamily
Article first published online: 8 APR 2013
© 2013 The Authors Journal compilation © 2013 FEBS
Volume 280, Issue 11, pages 2622–2632, June 2013
How to Cite
Lee, Y., Mehra-Chaudhary, R., Furdui, C. and Beamer, L. J. (2013), Identification of an essential active-site residue in the α-d-phosphohexomutase enzyme superfamily. FEBS Journal, 280: 2622–2632. doi: 10.1111/febs.12249
- Issue published online: 23 MAY 2013
- Article first published online: 8 APR 2013
- Accepted manuscript online: 20 MAR 2013 09:26AM EST
- Manuscript Accepted: 14 MAR 2013
- Manuscript Revised: 12 MAR 2013
- Manuscript Received: 31 DEC 2012
- US National Science Foundation. Grant Number: MCB-0918389
|febs12249-sup-0001-FigS1-S2-TableS1.zip||Zip archive||1939K|| |
Fig. S1. Sequence alignment of proteins in the α-d-phosphohexomutase superfamily.
Fig. S2. Schematic showing the reaction of PMM/PGM with the proposed roles of His329 as a general base and Arg20 as a general acid.
Table S1. Distances between protein residues and sites of action for putative general base and general acid in enzyme-ligand complexes of P. aeruginosa PMM/PGM.
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