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. Author manuscript; available in PMC: 2012 Dec 1.
Published in final edited form as: Clin Biochem. 2011 Oct 6;44(17-18):1434–1439. doi: 10.1016/j.clinbiochem.2011.09.016

Table 1.

Screening of Fluorescent Substrate Cleavage Activity by MMPs and ADAMs

Flsub10c Flsub21b Flsub13b Flsub63a Flsub8b Flsub11a
ADAM8 3.3 × 104 1.0 × 105 5.3 × 104 2.5 × 103 1.7 × 103 2.4 × 103
ADAM9 1.1 × 105 8.3 × 103 1.6 × 103 2.2 × 104 4.5 × 103 2.3 × 102
ADAM10 3.6 × 103 6.2 × 103 2.7 × 102 1.4 × 104 1.9 × 102 <1 × 101
ADAM12 3.8 × 104 2.8 × 105 4.0 × 101 NAd 3.0 × 103 NAd
ADAM17 9.6 × 105 4.3 × 105 NDe 1.1 × 103 3.8 × 104 3.7 × 103
MMP-1 5.1 × 104 2.8 × 104 NDe 3.2 × 103 7.6 × 104 4.5 × 104
MMP-2 1.7 × 105 3.2 × 105 2.4 × 103 1.3 × 106 2.9 × 104 4.8 × 105
MMP-3 3.9 × 104 4.0 × 103 NDe 2.2 × 104 5.2 × 101 1.6 × 103
MMP-8 2.6 × 104 1.4 × 105 NDe 3.4 × 105 2.4 × 104 3.6 × 104
MMP-9 6.0 × 105 2.2 × 105 NDe 1.4 × 105 8.5 × 105 1.4 × 106
MMP-13 1.7 × 106 4.6 × 105 NDe 1.6 × 106 2.1 × 106 3.3 × 106
a

Specificity values at 10 µM substrate concentration were measured by back calculation of enzyme concentrations after determination of kcat/Km for known substrates. Enzyme concentrations were determined previously by active site titration as described in Rasmussen et. al. [34]

b

Values were taken from Moss et. al. [35]

c

Values were taken from Moss et. al. [42]

d

Not attempted

e

No activity detected