Mode of action of bacterial collagenase on a synthetic substrate, (Pro-Pro-Gly)5

  • Oshima G
  • Shimabukubo H
  • Nagasawa K
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Abstract

Clostridial collagenase (EC 3.4.24.3) catalyzes the hydrolysis of (Pro-Pro-Gly)5at a 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 chromatography 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- > deca- > and nona- > 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. © 1979.

Author-supplied keywords

  • (Bacterial)
  • (Pro-Pro-Gly)5
  • Collagenase
  • Mechanism
  • Synthetic substrate

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Authors

  • Genichiro Oshima

  • Hirokazu Shimabukubo

  • Kinzo Nagasawa

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