Catalytic domain comparisons of human fibroblast-type collagenase, stromelysin-1, and matrilysin

L. Jack Windsor, Darin L. Steele, Susan B. LeBlanc, Kenneth B. Taylor

Research output: Contribution to journalArticle

11 Scopus citations


The propeptide plus the catalytic domain of human fibroblast-type collagenase, stromelysin-1, and matrilysin were expressed in Escherichia coli to directly compare the properties of all three catalytic domains utilizing the same assays. Truncated fibroblast-type collagenase (mini-CL), truncated stromelysin-1 (mini-SL-1), and matrilysin, like their native counterparts, could be activated by organomercurials, trypsin, or SDS. The mini-CL and mini-SL-1 displayed catalytic properties similar to their native counterparts, except that the mini-CL could not cleave native type I collagen. The k(cat)/K(m) for matrilysin (355 μM-1 h-1) on the synthetic Mca-peptide was much higher than that for mini-CL (69 μM-1 h-1) or mini-SL-1 (23.6 μM-1 h-1). Mini-SL-1 and matrilysin, but not mini-CL, were capable of superactivating collagenase thus increasing the rate of collagen cleavage. Mini-CL and mini-SL-1, but not matrilysin, were able to form SDS-stable complexes with TIMP-1 when co-incubated with an organomercurial and TIMP-1. The second-order rate constant (k(on)) for TIMP-1 inhibition of mini-CL and mini-SL-1 were similar, 0.635 · 105 M-1 s-1 and 1.52 · 105 M-1 s-1, respectively. The k(on) for TIMP-1 inhibition of matrilysin was lower (0.130 · 105 M-1 s-1) supporting the observation that no SDS stable complexes were detected. This study demonstrates that these catalytic domains are distinct and play a major role in the specificity of these enzymes in regard to rate of catalysis, TIMP-1 binding, and superactivation of collagenase.

Original languageEnglish (US)
Pages (from-to)261-272
Number of pages12
JournalBiochimica et Biophysica Acta - General Subjects
Issue number2-3
StatePublished - Mar 15 1997
Externally publishedYes


  • Collagenase
  • Matrilysin
  • Matrix metalloproteinase
  • Stromelysin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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