Functional tyrosine residues in rabbit liver cathepsin d modification by tetranitromethane
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Tetranitromethane
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The lysosomal cysteine proteinase cathepsin B (from human liver) was tested for its peptide-bond specificity against the oxidized B-chain of insulin. Sixteen peptide degradation products were separated by high-pressure liquid chromatography and thin-layer chromatography and were analysed for their amino acid content and N-terminal amino acid residue. Five major and six minor cleavage sites were identified; the major cleavage sites were Gln(4)-His(5), Ser(9)-His(10), Glu(13)-Ala(14), Tyr(16)-Leu(17) and Gly(23)-Phe(24). The findings indicate that human cathepsin B has a broad specificity, with no clearly defined requirement for any particular amino acid residues in the vicinity of the cleavage sites. The enzyme did not display peptidyldipeptidase activity with this substrate, and showed a specificity different from those reported for two other cysteine proteinases, papain and rat cathepsin L.
Cleavage (geology)
Cathepsin H
Cathepsin A
Peptide bond
Cathepsin L
Residue (chemistry)
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Some physicochemical properties of the cathepsin D purified from the rabbit muscle (L. dorsi) were investigated. The sedimentation coefficient (s20,w) and the molecular weight determined from sedimentation equilibrium experiment was 3.83 S and 29,000~30,000, respectively. The amino acid composition of the enzyme was determined with an automatic amino acid analyzer. The proteolytic specificity of the enzyme was also investigated using the B-chain of oxidized beef insulin as the substrate. The cathepsin D cleaved the bonds Phe-Val, Ala-Leu, Leu-Tyr and Tyr-Leu. The specificity of the cathepsin D was fairly similar to that of the pepsin.
Proteolysis
Pepsin
Sedimentation equilibrium
Peptide bond
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Action of cathepsin H from bovine spleen on tuftsin, enkephalin, the oxidized B chain of insulin and a variety of synthetic substrates was studied. Cathepsin H splits off only one N-terminal amino acid from each tuftsin and enkephalin, which, according to the literature, led to inactivation of peptides. The enzyme acts on the oxidized B chain of insulin as an aminoendopeptidase: it splits off the N-terminal phenylalanine and the centrally located bond(s). Km and Vmax for the cathepsin H catalyzed hydrolysis of LeuNA, ArgNA LysNA and BANA were determined. Substrates with the free NH2 group were hydrolyzed at a higher rate. Based on the data obtained and the previously reported results on conversion of kallidin into bradykinin, the specificity of cathepsin H and its possible biological functions were discussed. Cathepsin H appears to participate in formation and inactivation of physiologically active peptides. Using the antiserum to spleen cathepsin H it was found that liver, kidney and lung tissues contained the enzymes identical and/or partially identical to cathepsin H from spleen. The data on the properties of cathepsin H from various sources are summarized.
Kallidin
Cathepsin H
Tuftsin
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The interaction of human recombinant full‐length cathepsin S propeptide (amino acids 16–114) with mature cysteine proteinases was studied with respect to selectivity and pH dependence. The inhibitory capacity was tested towards mature human recombinant cathepsin S, purified cathepsin L from rat and Paramecium tetraurelia , rat cathepsin B, human cathepsin H, and papain. The propeptide of cathepsin S strongly inhibited cathepsin S ( K i = 0.27 nM) and the two cathepsin L species ( K t = 0.36 nM) at neutral pH. Papain, and to a minor extent cathepsin H, hydrolyzed the propeptide of cathepsin S, leading to competition with the hydrolysis of the fluorogenic substrates in the respective assays. Cathepsin B activity was nearly unaffected up to micromolar propeptide concentrations in the assay. The inhibition of cath‐epsin‐L‐like peptidases was diminished with decreasing pH, probably due to dramatic changes in the conformation of the propeptide. This assumption was supported by far‐ultraviolet CD spectroscopy and by the finding of rapid hydrolysis of the cathepsin S propeptide by cathepsin L at pH values less than 5.5.
Cathepsin H
Cathepsin A
Protein precursor
Cathepsin L
Cathepsin E
Cathepsin L1
Cathepsin S
Cathepsin C
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Journal Article Purification and Processing of Rat Liver Procathepsin B Get access Takahiro Kawabata, Takahiro Kawabata Division of Physiological Chemistry, Faculty of pharmacetutical Sciences, Kyusha University,Higashi-ku, Fukuoha 812 Search for other works by this author on: Oxford Academic PubMed Google Scholar Yukio Nishimura, Yukio Nishimura Division of Physiological Chemistry, Faculty of pharmacetutical Sciences, Kyusha University,Higashi-ku, Fukuoha 812 Search for other works by this author on: Oxford Academic PubMed Google Scholar Masahide Higaki, Masahide Higaki Division of Physiological Chemistry, Faculty of pharmacetutical Sciences, Kyusha University,Higashi-ku, Fukuoha 812 Search for other works by this author on: Oxford Academic PubMed Google Scholar Keitaro Kato Keitaro Kato 2 Division of Physiological Chemistry, Faculty of pharmacetutical Sciences, Kyusha University,Higashi-ku, Fukuoha 812 2To whom correspondence should be addresed. Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 113, Issue 3, March 1993, Pages 389–394, https://doi.org/10.1093/oxfordjournals.jbchem.a124056 Published: 01 March 1993 Article history Received: 04 November 1992 Published: 01 March 1993
Pepstatin
Sepharose
Cathepsin H
Cathepsin C
Cathepsin L1
Cathepsin A
Cathepsin L
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Treatment of a native protein inhibitor of proteinases by tetranitromethane results inmodification of 3 (out of 8) tyrosine residues in each of the two subunits within the inhibitor molecule. Nitration of surface tyrosines does not change the corformation of the protein and has no effect on its ability to inhibit chymotrypsin. At the same time the tetranitromethane-treated inhibitor possesses a decreased activity with respect to trypsin. In the presence of 0,5 M DS-Na practically all tyrosine residues of the protein are nitrated.
Tetranitromethane
Trypsin inhibitor
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The exchange of residues 67 and 205 of the S2 pocket of human cysteine cathepsins K and L induces a permutation of their substrate specificity toward fluorogenic peptide substrates. While the cathepsin L-like cathepsin K (Tyr67Leu/Leu205Ala) mutant has a marked preference for Phe, the Leu67Tyr/Ala205Leu cathepsin L variant shows an effective cathepsin K-like preference for Leu and Pro. A similar turnaround of inhibition was observed by using specific inhibitors of cathepsin K [1-(N-Benzyloxycarbonyl-leucyl)-5-(N-Boc-phenylalanyl-leucyl)carbohydrazide] and cathepsin L [N-(4-biphenylacetyl)-S-methylcysteine-(D)-Arg-Phe-beta-phenethylamide]. Molecular modeling studies indicated that mutations alter the character of both S2 and S3 subsites, while docking calculations were consistent with kinetics data. The cathepsin K-like cathepsin L was unable to mimic the collagen-degrading activity of cathepsin K against collagens I and II, DQ-collagens I and IV, and elastin-Congo Red. In summary, double mutations of the S2 pocket of cathepsins K (Y67L/L205A) and L (L67Y/A205L) induce a switch of their enzymatic specificity toward small selective inhibitors and peptidyl substrates, confirming the key role of residues 67 and 205. However, mutations in the S2 subsite pocket of cathepsin L alone without engineering of binding sites to chondroitin sulfate are not sufficient to generate a cathepsin K-like collagenase, emphasizing the pivotal role of the complex formation between glycosaminoglycans and cathepsin K for its unique collagenolytic activity.
Cathepsin A
Cathepsin C
Cathepsin E
Cathepsin H
Cathepsin S
Cathepsin L
Cathepsin K
Cathepsin L1
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The mechanism of degradation of fructose-1,6-bisphosphate aldolase from rabbit muscle by the lysosomal proteinase cathepsin B was determined. Treatment of aldolase with cathepsin B destroys up to 90% of activity with fructose 1,6-bisphosphate as substrate, but activity with fructose 1-phosphate is slightly increased. Cathepsin L, another lysosomal thiol proteinase, and papain are also potent inactivators of aldolase, whereas inactivation is not caused by cathepsins D or H even at high concentrations, or by cathepsin B inhibited by leupeptin or iodoacetate. The cathepsin-B-treated aldolase shows no detectable change in subunit molecular weight, oligomer molecular weight or subunit interactions. Cathepsin B cleaves dipeptides from the C-terminus of th aldolase subunits. Four dipeptides are released sequentially: Ala-Tyr, Asn-His, Ile-Ser and Leu-Phe, and a maximum of five additional dipeptides may be released. There are indications that this peptidyldipeptidase activity of cathepsin B may be an important aspect of its action on protein substrates generally.
Aldolase B
Cathepsin H
Cathepsin A
Cathepsin C
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Thiol
Protein primary structure
Cathepsin L
Sequence (biology)
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The selective cleavage of peptide bonds by cathepsin L from rat liver was examined with a hexapeptide, luteinizing hormone releasing hormone, neurotensin and oxidized insulin A chain as model substrates. The specificity of cathepsin L was compared with that of cathepsin B. Cathepsin L cleaved peptide bonds that have a hydrophobic amino acid, such as Phe, Leu, Val, and Trp or Tyr, in position P2. A polar amino acid, such as Tyr, Ser, Gly, Glu, Asp, Gln, or Asn, in position P1. enhanced the susceptibility of the peptide bond to cathepsin L, though the importance of the amino acid residue in position P1' was not as great as that of the amino acid in position P2 for the action of cathepsin L. These results suggest that, in contrast to cathepsin B, cathepsin L shows very clear specificity.
Peptide bond
Cleavage (geology)
Cathepsin H
Cathepsin A
Cathepsin L1
Cathepsin E
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