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PMID: 6574504 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 80 ·No. 12 ·1983-06-00 ·Pages 3666-70

Takio K, Towatari T, Katunuma N, Teller DC, Titani K

Abstract

The amino acid sequences of rat liver lysosomal thiol endopeptidases, cathepsins B and H, are presented and compared with that of the plant thiol protease papain. The 252-residue sequence of cathepsin B and the 220-residue sequence of cathepsin H were determined largely by automated Edman degradation of their intact polypeptide chains and of the two chains of each enzyme generated by limited proteolysis. Subfragments of the chains were produced by enzymatic digestion and by chemical cleavage of methionyl and tryptophanyl bonds. Comparison of the amino acid sequences of cathepsins B and H with each other and with that of papain demonstrates a striking homology among their primary structures. Sequence identity is extremely high in regions which, according to the three-dimensional structure of papain, constitute the catalytic site. The results not only reveal the first structural features of mammalian thiol endopeptidases but also provide insight into the evolutionary relationships among plant and mammalian thiol proteases.

MeSH Terms
Amino Acid Sequence Animals Cathepsin B Cathepsin H Cathepsins Cyanogen Bromide Cysteine Endopeptidases Liver/enzymology Models, Molecular Papain Peptide Fragments/analysis Protein Conformation Rats
Chemicals
Peptide Fragments Cathepsins Cysteine Endopeptidases Cathepsin B Cathepsin H Ctsh protein, rat Papain Cyanogen Bromide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Takio K
Towatari T
Katunuma N
Teller D C
Titani K
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37 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.80.12.3666
Published
1983-06-00
Pages
3666-70
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC394111
Subset
IM
Grants
NIGMS NIH HHS · GM 13401 · United States
NIGMS NIH HHS · GM 15731 · United States
External Links
PubMed source DOI: 10.1073/pnas.80.12.3666 PMC Full Text View journal details
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