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3.4.22.1: cathepsin B

This is an abbreviated version!
For detailed information about cathepsin B, go to the full flat file.

Word Map on EC 3.4.22.1

Reaction

Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides =

Synonyms

AC-5, AC-cathB-1, AC-cathB-2, APP secretase, cat B, CatB, CatB1, Cath B, Cath-B, CathB, cathepsin B, cathepsin B proteinase, cathepsin B-like AC-5, cathepsin B-like counter-defence protein, cathepsin B-like cysteine protease, cathepsin B-like cysteine protease 1, cathepsin B-type cysteine protease, cathepsin B1, cathepsin B2, cathepsin B5, cathepsin Ba, cathepsin II, cathepsin-B, CmCatB1, CmCatB2, CP-2, CPB, CpCathB, CPR-4, CsCB1, CsCB2, CsCB3, CsCB4, CTB, CTSB, cysteine cathepsin, DEVDase, LycCatB, MmeCB, More, Na-CP-2, Na-CP-3, Na-CP-4, Na-CP-5, NbCathB, nfcpb, nfcpb-L, PcCTSB, rFgCatB2, Sm31, SmCatB, SmCB1, toxopain-1, TrCB1.1, TrCB1.2, TrCB1.3, TrCB1.4, TrCB1.5, TrCB1.6, TsCPB2

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.1 cathepsin B

pH Range

pH Range on EC 3.4.22.1 - cathepsin B

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 4
-
collagen as substrate
3 - 6
pH 3.0: about75 % of maximal activity, pH 6.0: about 50% of maximal activity
3.5 - 6.5
-
activity range with substrate acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin, about 90% of maximal activity at pH 3.5, maximal activity at pH 4.0, and about 5-10% of maximal activity at pH 6.5, iactive at pH 7.0
4 - 6
4 - 6.5
4 - 7
4 - 8
-
FhcatB1is active across a broad pH range, approximately 30-80% of maximal activity at pH 5.0 and pH 8.0
4 - 8.5
-
-
4.5 - 5.5
-
maxinal activity at pH 4.5, inactivation at pH 5.5 and inactive above
4.5 - 6
-
the protease activity is stable in the acidic range between pH 4.5 and 6.0, and declines above pH 6.5 rapidly. At pH 6.5, more than 60% of the enzyme activity is lost
4.5 - 7
4.8 - 7.4
-
activity measurement range, vesicle-associated cathepsin B activity is increased 1300fold at acidic pH values compared to physiological pH 7.4, cathepsin B activity in cell extract is increased 33fold at pH 5.6 versus pH 7.4
5 - 6
pH 5.0: 82% of maximal activity, pH 6.0: 80% of maximal activity
5 - 6.5
more than 60% of maximum activity in the pH range of 5.0-6.5
5 - 7
5.5 - 7
7.5
-
irreversible unfolding of native enzyme, mutant C29A is stable
8
-
half-life of wild type enzyme 84 s, mutant H110A 22 s, mutant H111A 75 s