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Literature summary extracted from

  • Camp, R.J.; Liles, M.; Beale, J.; Saeidi, N.; Flynn, B.P.; Moore, E.; Murthy, S.K.; Ruberti, J.W.
    Molecular mechanochemistry: low force switch slows enzymatic cleavage of human type I collagen monomer (2011), J. Am. Chem. Soc., 133, 4073-4078.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.3 Hathewaya histolytica
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.3 Collagen type I + H2O tensile loads higher than 3 pN tenfold reduce the enzymatic degradation rate of recombinant human type I collagen monomers compared to unloaded controls. Collagen molecular architecture may be generally more stable when mechanically strained in tension. The tensile mechanical state of collagen monomers is likely to be correlated to their longevity in tissues Hathewaya histolytica ?
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