Literature summary for 3.4.21.4 extracted from

Lindstad, R.I.; Sylte, I.; Mikalsen, S.O.; Seglen, P.O.; Berg, E.; Winberg, J.O.
Pancreatic trypsin activates human promatrix metalloproteinase-2 (2005), J. Mol. Biol., 350, 682-698.

Search for more literature for 3.4.21.4

Activating Compound

Activating Compound	Comment	Organism	Structure
EDTA	increase in activation of pro-matrix metalloproteinase-2	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
tissue inhibitor of matrix metalloproteinases-2	TIMP-2, prevents the C-terminal truncation of activated metalloproteinase-2, without affecting the generation of the initial 62 kDa activated species	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	commercial preparation	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pro-matrix metalloproteinase-2 + H2O	activation by trypsin depends on various factors such as the level of exogenously added Ca2+ and Brij-35, temperature, and trypsin concentration. Activation occurs as sequential processing, initially generating an active 62 kDa species followed by successive truncation of the C-terminal domain leading to active species of 56 kDa, 52 kDa and 50kDa. Comparison with activation of pro-matrix metalloproteinase-2 by membrane-type 1 metalloproteinase or 4-aminophenylmercuric acetate	Sus scrofa	matrix metalloproteinase-2 + pro-peptide	-	?

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Release 2023.1 (January 2023)