Literature DB >> 3342889

Amino acid sequences of the human kidney cathepsins H and L.

A Ritonja1, T Popović, M Kotnik, W Machleidt, V Turk.   

Abstract

The complete amino acid sequences of human kidney cathepsin H (EC 3.4.22.16) and human kidney cathepsin L (EC 3.4.22.15) were determined. Cathepsin H contains 230 residues and has an Mr of 25116. The sequence was obtained by sequencing the light, heavy and mini chain and the peptides produced by cyanogen bromide cleavage of the single-chain form of the enzyme. The glycosylated mini chain is a proteolytic fragment of the propeptide of cathepsin H. Human cathepsin L has 217 amino acid residues and an Mr of 23720. Its amino acid sequence was deduced from N-terminal sequences of the heavy and light chains and from the sequences of cyanogen bromide fragments of the heavy chain. The fragments were aligned by comparison with known sequences of cathepsins H and L from other species. Cathepsins H and L exhibit a high degree of sequence homology to cathepsin B (EC 3.4.22.1) and other cysteine proteinases of the papain superfamily.

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Year:  1988        PMID: 3342889     DOI: 10.1016/0014-5793(88)80028-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  15 in total

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Review 5.  Cathepsin B: multiple roles in cancer.

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Authors:  H J Linthorst; C van der Does; J A van Kan; J F Bol
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9.  A thiol protease and an anionic peroxidase are induced by lowering cytokinins during callus growth in Petunia.

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10.  Preventing Cleavage of the Respiratory Syncytial Virus Attachment Protein in Vero Cells Rescues the Infectivity of Progeny Virus for Primary Human Airway Cultures.

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