Literature summary for 3.4.22.34 extracted from

Elsaesser, B.; Zauner, F.B.; Messner, J.; Soh, W.T.; Dall, E.; Brandstetter, H.
Distinct roles of catalytic cysteine and histidine in the protease and ligase mechanisms of human legumain as revealed by DFT-based QM/MM simulations (2017), ACS Catal., 7, 5585-5593 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q99538	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the cysteine protease enzyme legumain hydrolyzes peptide bonds with high specificity after asparagine and under more acidic conditions after aspartic acid. Legumain additionally exhibits ligase activity that prevails at pH above 5.5. Ligation is not the exact reverse of the proteolysis but can proceed via two distinct routes. Whereas the transpeptidation route involves aminolysis of the thioester, at pH 6 a cysteine-independent, histidine-assisted ligation route is detected	Homo sapiens	?	-	?

General Information

General Information	Comment	Organism
physiological function	important roles in immunity, cancer, and neurodegenerative diseases	Homo sapiens

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Release 2023.1 (January 2023)