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. Author manuscript; available in PMC: 2010 May 1.
Published in final edited form as: J Immunol. 2009 May 1;182(9):5770–5777. doi: 10.4049/jimmunol.0900127

Table I.

Kinetic comparisons of peptidyl nitroanilide hydrolysis by chymotryptic peptidases

AAPF-4NA AEPF-4NA RETF-4NA VPF-4NA

Chymase kcata 9.3 ± 0.8 8.8 ± 0.2 19.7 ± 0.1 17.2 ± 0.4
Kma 0.31 ± 0.07 0.15 ± 0.01 0.64 ± 0.05 0.29 ± 0.04
kcat/Kma 30 59 31 59

+ α2M kcat 49 ± 2 51 ± 1 87 ± 1 8.9 ± 0.6
Km 0.28 ± 0.02 0.08 ± 0.08 0.32 ± 0.01 0.16 ± 0.03
kcat/Km 170 640 270 55

Cathepsin G kcat 1.4 ± 0.1 3.7 ± 0.8 7.3 ± 11.9 13.8 ± 0.4
Km 0.97 ± 0.06 0.93 ± 0.08 13 ± 36 0.69 ± 0.07
kcat/Km 1.4 3.9 0.56 20

+ α2M kcat 0 ± 0 0.71 ± 0.26 0 ± 0 2.4 ± 2.1
Km - 0.12 ± 0.15 - 0.8 ± 1.4
kcat/Km - 5.9 - 3.0

Chymotrypsin kcat 68 ± 8 12.8 ± 0.5 5.0 ± 0.4 11.8 ± 0.4
Km 0.52 ± 0.14 0.39 ± 0.04 1.1 ± 0.2 0.07 ± 0.01
kcat/Km 130 33 4.5 170

+ α2M kcat 48 ± 1 31 ± 1 3.9 ± 0.4 22 ± 1
Km 0.035 ± 0.003 0.17 ± 0.02 0.057 ± 0.026 0.037 ± 0.007
kcat/Km 1400 180 68 59
a

Units of turnover number kcat, Michaelis constant Km and specificity constant kcat/Km are s−1, mM, and s−1 mM−1, respectively