Enzymatic hydrolysis of β-mannosides was predicted to occur via an unusual boat transition state conformation. Structural and biochemical studies on transition state mimics of a retaining β-mannosidase now provide evidence for the predicted B2,5 transition state conformation.
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References
Herscovics, A. Biochim. Biophys. Acta 1473, 96–107 (1999).
Dhawan, S. & Kaur, J. Crit. Rev. Biotechnol. 27, 197–216 (2007).
Tailford, L.N. et al. Nat. Chem. Biol. 4, 306–312 (2008).
Pauling, L. Nature 161, 707–709 (1948).
Wolfenden, R. & Snider, M.J. Acc. Chem. Res. 34, 938–945 (2001).
Schramm, V.L. J. Biol. Chem. 282, 28297–28300 (2007).
Sinnott, M.L. Chem. Rev. 90, 1171–1202 (1990).
Ducros, V.M.-A. et al. Angew. Chem. Int. Ed. 41, 2824–2827 (2002).
Shah, N., Kuntz, D.A. & Rose, D.R. Biochemistry 42, 13812–13816 (2003).
Numao, S., Kuntz, D.A., Withers, S.G. & Rose, D.R. J. Biol. Chem. 278, 48074–48083 (2003).
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Palcic, M. β-Mannoside hydrolysis goes by boat. Nat Chem Biol 4, 269–270 (2008). https://doi.org/10.1038/nchembio0508-269
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DOI: https://doi.org/10.1038/nchembio0508-269
