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. Author manuscript; available in PMC: 2008 Oct 17.
Published in final edited form as: Biochemistry. 2007 Mar 6;46(12):3724–3733. doi: 10.1021/bi062199j

Figure 4. Flowchart depicting MMP triple-helical peptidase activities.

Figure 4

The 10 MMPs examined in the present study are initially sub-divided based upon their ability to cleave a triple-helical substrate. A sub-division within the triple-helical peptidase MMPs occurs upon their ability to process more thermally stable substrates. The sequence specificity of each MMP, initially based upon individual substitutions within the P1’ and P2 subsites (9), allows for the next sub-division. The sequence specificity of each MMP, based upon combined substitutions within the P1’ and P2 subsites, followed by preferences for an interrupted sequence, allows for a final sub-division. Ultimately, all “collagenolytic” MMPs (MMP-1, MMP-2, MP-8, MMP-13, MT1 MMP, and MT2-MMP) display distinct behaviors.