Comparison of the
Catalytic Domains of Collagenase-1 and Stromelysin-1
HU Liang-Yan1, TIAN Shao-Min, YE Qi-Zhuang1,
RUAN Kang-Cheng*
( Shanghai Institute of Biochemistry, Shanghai Institutes for Biological
Sciences, the Chinese Academy of Sciences, Shanghai 200031, China； 1Shanghai Institute of Medicine, Shanghai
Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China )
Abstract The
catalytic domains of two matrix metalloproteinases―collagenase-1 and
stromelysin-1 have been studied by means of fluorescence spectroscopy and high
hydrostatic pressure. The hydrophobic fluorescence probe ANS could bind to
stromelysin-1, with a dissociation constant of 26.3 μmol/L, but could not bind
to collagenase-1, indicating that there exists a hydrophobic site on the
surface of stromelysin-1. Further study suggests that the hydrophobic site may
not be the catalytic site. The biological activity of catalytic domains of
collagenase-1 and stromelysin-1 showed obvious difference under high pressure： the activity of collagenase-1
increased with elevating pressure, with an activation volume of �D18.9 ml/mol； however, the activity of
stromelysin-1 did not change under high pressure. The results indicate that there
are some obvious differences between the catalytic domain conformations of
these two enzymes, though the crystal analysis indicated that they were very
similar as reported before.
Key words matrix metalloproteinase； collagenase-1； stromelysin-1； high pressure； ANS
*Corresponding author： Tel, 86-21-64740532； Fax 86-21-64338357； e-mail, [email protected]