Sequence of CATL3_PARTE
EC Number:3.4.22.15
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity
Other sequences found for EC No. 3.4.22.15
General information:
Sequence
0 MKQFLTAAIV TLLMTAGYYH LQEDDTNDFE RWALKNNKFY TESEKLYRME IYNSNKRMIE
60 EHNQREDVTY QMGENQFMTL SHEEFVDLYL QKSDSSVNIM GASLPEVQLE GLGAVDWRNY
120 TTVKEQGQCA SGWAFSVSNS LEAWYAIRGF QKINASTQQI VDCDYNNTGC SGGYNAYAME
180 YVLRVGLVSS TNYPYVAKNQ TCKQSRNGTY FINGYSFVGG SQSNLQYYLN NYPISVGVEA
240 SNWQFYRSGL FSNCSSNGTN HYALAVGFDS ANNWIVQNSW GTQWGESGNI RLYPQNTCGI
300 LNYPYQVY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
141185
Aury J.-M.,Jaillon O.,Duret L.,Noel B.,Jubin C.,Porcel B.M.,Segurens B.,Daubin V.,Anthouard V.,Aiach N.,Arnaiz O.,Billaut A.,Beisson J.,Blanc I.,Bouhouche K.,Camara F.,Duharcourt S.,Guigo R.,Gogendeau D.,Katinka M.,Keller A.-M.,Kissmehl R.,Klotz C.,Koll F.,Le Mouel A.,Lepere G.,Malinsky S.,Nowacki M.,Nowak J.K.,Plattner H.,Poulain J.,Ruiz F.,Serrano V.,Zagulski M.,Dessen P.,Betermier M.,Weissenbach J.,Scarpelli C.,Schaechter V.,Sperling L.,Meyer E.,Cohen J.,Wincker P.
Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia.
Nature
444
171-178
2006
141186
Voelkel H.,Kurz U.,Linder J.,Klumpp S.,Gnau V.,Jung G.,Schultz J.E.
Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia: purification, cloning, sequencing and specific inhibition by its expressed propeptide.
Eur. J. Biochem.
238
198-206
1996
