3.4.22.B6: cathepsin B-like protease
This is an abbreviated version!
For detailed information about cathepsin B-like protease, go to the full flat file.
Reaction
the enzyme does not readily hyrolyze benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin (which is cleaved by cathespsin B). The enzyme is not able to cleave synthetic substrates having an Arg in position P2
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Synonyms
AC-5 cathepsin B-like protease, CatB, CatB2, CathB-1, CathB2, CathB3, cathepsin B type protease, cathepsin B-like cysteine protease, cathepsin B-like cysteine protease 1, cathepsin B-like cysteine protease 2, cathepsin B-like cysteine proteinase, cathepsin B-like cysteine proteinase 1, cathepsin B-like cysteine proteinase 2, cathepsin B-like peptidase, cathepsin B-like protease, CBc1, CBc6, CBL1, CmCatB, CmCatB1, CmCatB2, CPB, CPC, CPC protease, eimeripain, HCB, LmacatB, LOC103512321, More, TbCatB, TcoCBc1, TcoCBc6, TrCB2
ECTree
Posttranslational Modification
Posttranslational Modification on EC 3.4.22.B6 - cathepsin B-like protease
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glycoprotein
sequence contains four potential N-glycosylation sites, two (Asn35, Asn72) present in the propeptide and the other two (Asn154, Asn313) located in the catalytic domain
proteolytic modification
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the enzyme is synthesized as preproprotein composed of a signal sequence, a proenzyme region , and a mature proteinase sequence
proteolytic modification
CathB2 is predicted to be synthesized as a 40-kDa preproenzyme of 362 amino acids, consisting of a 33-residue signal peptide, a latency-mediating proregion (72 amino acids) and the C-terminal catalytic domain (257 amino acids)
proteolytic modification
TcoCBc1 is able to autocatalyze its maturation 21 residues upstream of the predicted start of the catalytic domain
proteolytic modification
TcoCBc6 is able to autocatalyze its maturation 31 residues, upstream of the predicted start of the catalytic domain