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Collagen/collagenase interaction: Does the enzyme mimic the conformation of its own substrate?
Author(s) -
De Souza Sandro J.,
Pereira Humberto M.,
Jacchieri Saul,
Brentani Ricardo R.
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.8.8666171
Subject(s) - collagenase , chemistry , substrate (aquarium) , enzyme , biophysics , biochemistry , biology , ecology
In this report, we present a hypothesis on the mechanism used by interstitial collagenases to cleave their natural substrate, interstitial collagens. The hypothesis is based on the assumption that the proline hinge domain of interstitial collagenase adopts a collagen‐like conformation. With a colla‐ gen‐like domain, the enzyme is able to disturb the quaternary organization of the triple helix in the collagenase‐susceptible site. A modeling analysis suggests that interaction between prolines of both collagen and collagenase forming a kind of “proline zipper” is involved in the destabilization step. This destabilization makes the three‐collagen helix susceptible to the catalytic cleft of the catalytic core.—de Souza, S. J., Pereira, H. M., Jacchieri, S., Brentani, R. R. Collagen/collagenase interaction: Does the enzyme mimic the conformation of its own substrate? FASEB J. 10, 927‐930 (1996)