Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: Cloning, expression, enzymatic properties, and subsite identification

Table 2 The rate constants and the binding free energy changes estimated from the kinetic modeling calculation.

Substrate	Rate constant (s ^-1 )			Binding free energy ( k cal mol^-1)
	k ₊₁	k _-1	k ₊₂	(-2)	(-1)	(+1)	(+2)	(+3)	(+4)
GlcNAc_4-6	0.07-0.1	0.0	50.0	+7.0	-4.5	0.0	-1.1	-0.1	+0.9

The optimization was based on the experimental time-course of hexamer hydrolysis catalyzed VhNag2 (upper panels of Fig. 6).

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