| Literature DB >> 30091759 |
James Froberg1, Woo-Sik Choi, Abbas Sedigh, Tayebeh Anajafi, Jasmin Farmakes, Zhongyu Yang, Sanku Mallik, D K Srivastava, Yongki Choi.
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.Entities:
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Year: 2018 PMID: 30091759 PMCID: PMC6145137 DOI: 10.1039/c8cc04601h
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222