[HTML][HTML] Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase
JM Chen, PM Dando, ND Rawlings, MA Brown… - Journal of Biological …, 1997 - ASBMB
Legumain is a cysteine endopeptidase that shows strict specificity for hydrolysis of
asparaginyl bonds. The enzyme belongs to peptidase family C13, and is thus unrelated to
the better known cysteine peptidases of the papain family, C1 (Rawlings, ND, and Barrett, AJ
(1994) Methods Enzymol. 244, 461-486). To date, legumain has been described only from
plants and a blood fluke, Schistosoma mansoni We now show that legumain is present in
mammals. We have cloned and sequenced human legumain and part of pig legumain. We …
asparaginyl bonds. The enzyme belongs to peptidase family C13, and is thus unrelated to
the better known cysteine peptidases of the papain family, C1 (Rawlings, ND, and Barrett, AJ
(1994) Methods Enzymol. 244, 461-486). To date, legumain has been described only from
plants and a blood fluke, Schistosoma mansoni We now show that legumain is present in
mammals. We have cloned and sequenced human legumain and part of pig legumain. We …