3.4.22.1: cathepsin B

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

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

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Results	in table
113	Activating Compound
1179	AA Sequence
43	Application
1	CAS Registry Number
62	Cloned(Commentary)
9	Crystallization (Commentary)
7005	Disease/ Diagnostics
31	Expression
103	General Information
7	General Stability
260	IC50 Value
957	Inhibitors
32	kcat/KM [mM/s]
177	Ki Value [mM]
223	KM Value [mM]
126	Localization
3	Metals/Ions
104	Molecular Weight [Da]
115	Natural Substrates/ Products (Substrates)
5	Organic Solvent Stability
986	Organism
60	PDB ID
120	pH Optimum
32	pH Range
21	pH Stability
5	pI Value
38	Posttranslational Modification
61	Protein Variants
74	Purification (Commentary)
5	Reaction
2	Reaction Type
299	Reference
3	Renatured (Commentary)
440	Source Tissue
56	Specific Activity [micromol/min/mg]
5	Storage Stability
617	Substrates and Products (Substrate)
47	Subunits
199	Synonyms
70	Temperature Optimum [°C]
8	Temperature Range [°C]
16	Temperature Stability [°C]
54	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 3.4.22.1 - cathepsin B

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

13 entries

proteolytic modification

12 entries

side-chain modification

11 entries

additional information

Bos taurus

-

no redox regulation, enzyme is active over a broad redox potential range

650465

glycoprotein

Biomphalaria glabrata

A7LM75

-

699729

glycoprotein

Callosobruchus maculatus

B2XVS9, Q5VJM8

deglycosylation of recombinant CmCatB1 by N-glycosidase F

680163

glycoprotein

Callosobruchus maculatus

-

glycosylation at atypical Asn-X-Cys motif, non-canonical Asn-X-Cys sites, wild-type CatB contains three N-glycosylation Asn-X-Ser/Thr consensus sequences with existence of additional atypical glycosylation sites. The heterogeneously expressed CazB is also glycosylated in Pichia patoris. Residue Asn100 is responsible for non-canonical glycosylation. Glycosylation at the non-canonical Asn100 site decreases the proteolytic activity of CmCatB, while it enhances protein stability. Deglycosylation enhances CmCatB activity, but compromises CmCatB stability

708228

glycoprotein

Fasciola hepatica

-

the recombinant catB1 is mixed glycosylated

708747

glycoprotein

Homo sapiens

-

glycosylation at Ser115

698787

glycoprotein

Necator americanus

-

Na-CP-2 N-glycosylation site at position 140

700081

glycoprotein

Necator americanus

-

Na-CP-3 N-glycosylation site at positions 32, 136, 242, and 298

700081

glycoprotein

Necator americanus

-

Na-CP-4 N-glycosylation site at positions 134 and 296

700081

glycoprotein

Necator americanus

-

Na-CP-5 N-glycosylation site at positions 101, 135 and 245

700081

glycoprotein

Oreochromis niloticus

A0A2U8JGA6

the purified recombinant protein exhibiting the hydrolysis activity lacks the N-glycosylation site suggesting that the N-glycosylation site may have no obvious relation to the enzyme activity

753845

glycoprotein

Paralichthys olivaceus

Q68J69

the enzyme contains a conserved glycosylation site

698020

glycoprotein

Toxoplasma gondii

-

sequence contains two putative glycosilation sites

652276

glycoprotein

Trachurus japonicus

A0A0P0YP15

-

754582

proteolytic modification

Fasciola hepatica

-

the recombinant pro-catB1 is autoprocessed

708747

proteolytic modification

Homo sapiens

-

of C- and of N-terminus, autocatalytic processing, precursor forms are inactive

647962

proteolytic modification

Homo sapiens

-

autocatalytic activation of the purified proenzyme in 20 mM sodium acetate, pH 5.0, 1mM EDTA, for 5 days

698787

proteolytic modification

Homo sapiens

-

cathepsin B is secreted as an inactive precursor form and activated by cleavage through pepsin at pH 3.5

696518

proteolytic modification

Homo sapiens

-

cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively. Under certain conditions cathepsin-B may be secreted extracellularly as a pro-enzyme that requires proteolytic activation

698146

proteolytic modification

Homo sapiens

-

the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview

708489

proteolytic modification

Homo sapiens

P07858

cathepsin B is first expressed as a 44 kDa inactive precursor which then undergoes maturation to produce a 33 kDa lysosome enzyme later converted to a final active form composed of two (24 and 5 kDa) subunits

753138

proteolytic modification

Necator americanus

-

Na-CP-3 autoactivates by proteolytic cleavage at pH 4.0

700081

proteolytic modification

Nicotiana benthamiana

Q1HER6

the theoretical molecular mass of pro-NbCathB is 36700 Da, whereas that of the mature protease is 28600 Da

752850

proteolytic modification

Pandalus borealis

-

preproenzyme of 328 amino acids, comprising a 15-residue signal peptide, a 60-residue propeptide and a 253-residue mature enzyme

650893

proteolytic modification

Schistosoma mansoni

-

the protein is synthesized as a large 38 kDa precursor form which is proteolytically cleaved to yield a mature, active 31 kDa enzyme by the asparaginyl endopeptidase SmAE, i.e. schistosome legumain, SmAE is central to SmCB1 processing and activation

683858

proteolytic modification

Toxoplasma gondii

-

sequence contains a prepropeptide region

652276

side-chain modification

Artemia sp.

-

glycoprotein

36633

side-chain modification

Bubalus bubalis

-

glycoprotein

36657, 36658

side-chain modification

Bubalus bubalis

-

7% carbohydrate

36657

side-chain modification

Bubalus bubalis

-

3.6% carbohydrate

36658

side-chain modification

Capra hircus

-

glycoprotein

36651

side-chain modification

Capra hircus

-

6.3% carbohydrate

36652

side-chain modification

Homo sapiens

-

glycoprotein

34991

side-chain modification

Oryctolagus cuniculus

-

glycoprotein

36627

side-chain modification

Rattus norvegicus

-

glycoprotein

586915

side-chain modification

Rattus norvegicus

-

structure of carbohydrate moieties

586915

side-chain modification

Sus scrofa

-

glycoprotein

36624