Table 1.

Kinetic parameters and inhibition constants obtained by enthalpy array versus published values.

			Enthalpy Array			Literature values
Enzyme	Substrate	Inhibitor	KM (μM)	kcat (s−1)	KI (μM)	KM (μM)	kcat (s−1)	KI (μM)
Trypsin	BAEE	None	6.4 ±1.1	8.5 ±0.3		4a	15a		[11; 12]
Trypsin	BAEE	benzamidine			43 ±8b			20	[15]
Trypsin	BAEE	leupeptin			0.13 ±0.04c			0.15	[16]
PKA	Kemptide	None	16 ±4	8.5 ±0.5		5–16	11–14		[6; 23]
PKA	Kemptide	Ala-peptide			530 ±90b			320–490	[23; 29]
PKA	Kemptide	PKI-tide			0.66 ±0.04c			IC50= 0.2d	[32]
Hexokinase	ATP, (glucose)	None	180 ±30	250 ±10		95–200	270–450		[8;20;21; 22]
Hexokinase	glucose	None	94 ±8	250 ±10		84–167	270–450
Hexokinase	ATP, (fructose)	None	200 ±80	400 ±70		45–200	380–990e		[18;19; 21; 22]

Values reported are the average of at least three measurements with the standard error of the mean indicated.

^aK_M and k_cat for [BAEE]<1mM [12].

^bK_I values were derived using Equation (6), using the average value of K_M in the absence of inhibitor.

^cK_I values were derived using Equations (6)-(10), using the average value of K_M in the absence of inhibitor.

^dIC₅₀ value

^eReported as V_max relative to V_max glucose (1.4−2.2X).