Table 1.

Kinetic constants of the reactions between mesotrypsin and different Kunitz type inhibitors

Inhibitor	Ki	Ki (fold decrease)	kon	koff	kcata	kcat (fold decrease)
	m		m−1·s−1	s−1	s−1
APPIWT	(1.3 ± 0.2) × 10−7b,c		(2.4 ± 0.3) × 106i	(3.1 ± 0.02) × 10−1f	(35.6 ± 2.3) × 10−3c
APPII18F	(3.3 ± 0.2) × 10−9b,c		(5.9 ± 0.4) × 106i	(19.5 ± 0.7) × 10−3f	(10.4 ± 0.9) × 10−3c
APPIM17G/I18F/F34V	(9.8 ± 0.1) × 10−11f,g	34h	(5.0 ± 0.1) × 106g,i	(5.5 ± 0.1) × 10−4g,i	(4.3 ± 0.3) × 10−4c	24h
APPIT11C/M17G/I18F/F34C	(1.5 ± 0.1) × 10−7b		(4.1 ± 0.3) × 106i	(6.0 ± 0.04) × 10−1f	(5.2 ± 0.1) × 10−3
APPIM17C/I18F/F34C	(6.1 ± 0.1) × 10−11f	54h	(15.5 ± 0.2) × 106i	(1.0 ± 0.01) × 10−3i	(1.4 ± 0.02) × 10−4	74h
KD1TFPI1K15R	(4.2 ± 0.6) × 10−5b				(8.9 ± 0.1) × 10−1
KD1TFPI1K15R/I17C/I34C	(2.0 ± 0.1) × 10−7b	215h			(5.1 ± 0.1) × 10−2	17h
KD2Bikunin	(5. 1 ± 0.1) × 10−8b				(6.6 ± 0.4) × 10−3
KD2BikuninF17C/P34C	(4. 5 ± 0.1) × 10−8b	1.13h			(1.0 ± 0.1) × 10−3	6.6h

^a k_cat was determined by HPLC-based inhibitor cleavage time course.

^b Data were determined using Equation 1 (see “Experimental procedures”).

^c Results were taken from Ref. 19.

^d Data were determined using Equation 2 (see “Experimental procedures”).

^e Data were determined using Equation 3 (see “Experimental procedures”).

^f Data were determined using Equation 7 (see “Experimental procedures”).

^g Results were taken from Ref. 45.

^h Fold decrease relative to the parent protein scaffolds APPI_I18F, ^KD1TFPI1_K15R, or ^KD2bikunin.

ⁱ Data were determined using Equation 8 (see “Experimental procedures”).