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Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates.


ABSTRACT: The dynamic interactions of an individual matrix metalloproteinase-1 were imaged and monitored in the presence of either triple-helical or non-triple-helical, partially structured collagen-mimic substrates. The enzyme exhibited ten-fold increased catalytic turnover rates with the structurally modified substrate by skipping the triple-helix unwinding step during the catalytic pathway.

SUBMITTER: Froberg J 

PROVIDER: S-EPMC6145137 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates.

Froberg James J   Choi Woo-Sik WS   Sedigh Abbas A   Anajafi Tayebeh T   Farmakes Jasmin J   Yang Zhongyu Z   Mallik Sanku S   Srivastava D K DK   Choi Yongki Y  

Chemical communications (Cambridge, England) 20180901 73


The dynamic interactions of an individual matrix metalloproteinase-1 were imaged and monitored in the presence of either triple-helical or non-triple-helical, partially structured collagen-mimic substrates. The enzyme exhibited ten-fold increased catalytic turnover rates with the structurally modified substrate by skipping the triple-helix unwinding step during the catalytic pathway. ...[more]

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