3.4.22.B65: cathepsin P
This is an abbreviated version!
For detailed information about cathepsin P, go to the full flat file.
Word Map on EC 3.4.22.B65
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3.4.22.B65
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cathepsins
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papain
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peptidyl
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rodent
-
lysosomal
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proenzyme
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tubule
-
phe
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perimembranous
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kupffer
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cytred
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giant
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papain-like
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peptidases
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propeptide
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pecs
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rcho-1
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hepatocytes
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na2so4
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immunolocalization
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trophoblast
-
choriocarcinoma
-
preproprotein
- 3.4.22.B65
- cathepsins
- papain
-
peptidyl
- rodent
- lysosomal
- proenzyme
- tubule
- phe
-
perimembranous
-
kupffer
-
cytred
-
giant
-
papain-like
- peptidases
- propeptide
-
pecs
-
rcho-1
- hepatocytes
- na2so4
-
immunolocalization
-
trophoblast
- choriocarcinoma
- preproprotein
Reaction
Hydrolysis of proteins with restricted preference for substrates containing hydrophobic amino acids. Efficiently cleaves -Glu-Ile-Phe-/-Val-Phe-Lys-Gln-. Involved in the processing of endoplasmic proteins =
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Posttranslational Modification on EC 3.4.22.B65 - cathepsin P
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein
treatment of recombinant protein with PNGase F results in a single protein band of 29000 Da in SDS-PAGE for the zymogen and of 22000 Da for the autoactivated protein
proteolytic modification
the inactive zymogen can be activated by proteinase K, chymotrypsin or pancreatic elastase at neutral pH. Cathepsin P can be autoactivated at neutral pH, but not at acidic pH
