Literature summary for 3.4.21.5 extracted from

Robertson, A.L.; Headey, S.J.; Ng, N.M.; Wijeyewickrema, L.C.; Scanlon, M.J.; Pike, R.N.; Bottomley, S.P.
Protein unfolding is essential for cleavage within the alpha-helix of a model protein substrate by the serine protease, thrombin (2016), Biochimie, 122, 227-234 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00734	prothrombin	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
protein G + H2O	thrombin is able to cleave protein G, within its alpha-helix when a suitable cleavage sequence for the enzyme is introduced into this region. Thrombin is only cleaving within the alpha-helix when it is in an unfolded state. The introduction of destabilizing mutations within the protein increases the efficiency of cleavage by the enzyme	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)