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. Author manuscript; available in PMC: 2016 Jun 22.
Published in final edited form as: ACS Chem Biol. 2015 Mar 20;10(6):1495–1501. doi: 10.1021/cb500750v

Figure 5.

Figure 5

Hydrolysis of glycosidic bonds catalyzed by T4 lysozyme. The glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) subunits are depicted with one water molecule (black) surrounded by lysozyme’s key active-site functionalities Glu11, Asp20, and Thr26 (blue). The concerted mechanism shown with red arrows is observed in 90% of enzyme closures. Interruption of any step leads to the rarer, non-concerted mechanism, and causes the enzyme to pause in an intermediate, higher energy state. As described in the text, identical motions during re-opening suggest that the enzyme remains in the closed conformation during substrate translocation to an identical NAM-NAG glycosidic bond.