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Literature summary for 3.4.22.1 extracted from

  • Kirschke, H.; Wikstrom, P.; Shaw, E.
    Active center differences between cathepsins L and B the S, binding region (1988), FEBS Lett., 228, 128-130 .
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
2-naphthyl-alanine
-
Rattus norvegicus
4-nitro-L-phenylalanine inactivation rate is 3.0 mM/min Rattus norvegicus
citrulline
-
Rattus norvegicus
Cys (S-benzyl)
-
Rattus norvegicus
homophenylalanine
-
Rattus norvegicus
leupeptin leupeptin lacks selectivity since it inhibits both serine and cysteine proteases Rattus norvegicus
additional information inhibitory potency of a series benzyloxycarbonyl-Phe-X-diazomethylketone, in which Phe promotes binding at S2 while the amino acid X probes S1. The S1 region of cathepsin L also has the ability to accommodate large hydrophobic side chains. In this respect cathepsin L differs from cathepsin B. Thus benzyloxycarbonyl-Phe-Tyr(O-l-butyl)-diazomethylketone, inactivates cathepsin L with higher efficiency compared to cathepsin B Rattus norvegicus
Ser-(O-benzyl)
-
Rattus norvegicus
Thr (O-tert-butyl)
-
Rattus norvegicus
Trp inactivation rate is 12 mM/min Rattus norvegicus
Tyr-(O-methyl) inactivation rate is 1.548 mM/min Rattus norvegicus
Tyr-(O-tert-butyl) inactivation rate is 0.618 mM/min Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
Rattus norvegicus 5764
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P00787
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
cathepsin B
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
assay at Rattus norvegicus

General Information

General Information Comment Organism
additional information the substrate peptide bond cleaved by cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.15) is determined not by the amino acid contributing the carboxyl group to this bond as in the case of serine proteases but rather by the presence of a neighboring amino acid with a large hydrophobic side chain, active center differences between cathepsins L and B in the S1 binding region, overview Rattus norvegicus