Literature DB >> 3972105

Amino acid sequence of human liver cathepsin B.

A Ritonja, T Popovic, V Turk, K Wiedenmann, W Machleidt.   

Abstract

The complete amino acid sequence of cathepsin B (EC 3.4.22.1) from human liver was determined. The 252-residue sequence was obtained by automated solid-phase Edman degradation of the light and heavy chain resulting from limited proteolysis of the single-chain enzyme and of fragments produced by cyanogen bromide and enzymatic cleavage of the heavy chain. Human liver cathepsin B has 83.7% identical residues with the corresponding enzyme from rat liver. Comparison of both mammalian cathepsin B sequences with the sequence of papain provides further evidence that lysosomal and plant cysteine proteinases have evolved from a common ancestor and share a similar catalytic mechanism.

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Year:  1985        PMID: 3972105     DOI: 10.1016/0014-5793(85)81136-4

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


  15 in total

1.  Identification of lead compounds targeting the cathepsin B-like enzyme of Eimeria tenella.

Authors:  Marie Schaeffer; Joerg Schroeder; Anja R Heckeroth; Sandra Noack; Michael Gassel; Jeremy C Mottram; Paul M Selzer; Graham H Coombs
Journal:  Antimicrob Agents Chemother       Date:  2011-12-05       Impact factor: 5.191

2.  Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B.

Authors:  D Fong; D H Calhoun; W T Hsieh; B Lee; R D Wells
Journal:  Proc Natl Acad Sci U S A       Date:  1986-05       Impact factor: 11.205

3.  Purification of cathepsin B by a new form of affinity chromatography.

Authors:  D H Rich; M A Brown; A J Barrett
Journal:  Biochem J       Date:  1986-05-01       Impact factor: 3.857

4.  A catalytically active high-Mr form of human cathepsin B from sputum.

Authors:  D J Buttle; B C Bonner; D Burnett; A J Barrett
Journal:  Biochem J       Date:  1988-09-15       Impact factor: 3.857

5.  Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat cathepsin B C-terminal processing.

Authors:  A D Rowan; R Feng; Y Konishi; J S Mort
Journal:  Biochem J       Date:  1993-09-15       Impact factor: 3.857

6.  Human tumour cathepsin B. Comparison with normal liver cathepsin B.

Authors:  K Moin; N A Day; M Sameni; S Hasnain; T Hirama; B F Sloane
Journal:  Biochem J       Date:  1992-07-15       Impact factor: 3.857

7.  The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line.

Authors:  R W Mason; J E Walker; F D Northrop
Journal:  Biochem J       Date:  1986-12-01       Impact factor: 3.857

8.  Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization.

Authors:  H C Blair; S L Teitelbaum; L E Grosso; D L Lacey; H L Tan; D W McCourt; J J Jeffrey
Journal:  Biochem J       Date:  1993-03-15       Impact factor: 3.857

9.  Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

Authors:  S J Chan; B San Segundo; M B McCormick; D F Steiner
Journal:  Proc Natl Acad Sci U S A       Date:  1986-10       Impact factor: 11.205

10.  Identification of the active site residues in the nsP2 proteinase of Sindbis virus.

Authors:  E G Strauss; R J De Groot; R Levinson; J H Strauss
Journal:  Virology       Date:  1992-12       Impact factor: 3.616

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