Mode of action of bacterial collagenase on a synthetic substrate, (Pro-Pro-Gly)5.
Clostridial collagenase (EC 3.4.24.3) catalyzes the hydrolysis of (Pro-Pro-Gly)5 at minimum of three different rates, producing Pro-Pro, Gly-Pro-Pro and Gly-Pro-Pro-Gly, and various intermediate peptides. The intermediate and final products were separated by cation-exchange column chromatogrphy and identified, and their rates of formation were measured. Pro-Pro was released most rapidly with formation of the tridecapeptide. After the initial release of the N-terminal Pro-Pro, hexa- and heptapeptides were formed in larger amounts than tri-, tetra-, nona- and decapeptides from the tridecapeptide. The rates of disappearance of the intermediates decreased in the order trideca- greater than deca- and nona- greater than heptapeptide. The results indicate that the enzyme hydrolyzes inner linkages of the tridecapeptide having N- and C-terminal Gly residues, forming large peptides, preferentially to outer linkages, forming the tri- and tetrapeptides.
D003013:Clostridium / Q000201:enzymology*; D005998:Glycine; D003012:Microbial Collagenase / Q000378:metabolism*; D008954:Models, Biological; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D011392:Proline
D009842:Oligopeptides; D010455:Peptides; D011392:Proline; D003012:Microbial Collagenase; D005998:Glycine