Literature DB >> 6721861

Benzyloxycarbonylphenylalanylcitrulline p-nitroanilide as a substrate for papain and other plant cysteine proteinases.

C J Gray, J Boukouvalas, R J Szawelski, C W Wharton.   

Abstract

After preliminary assays, with papain, bromelain and ficin, on a range of citrulline p-nitroanilides, values of Km and kcat. for the papain-catalysed hydrolysis of three derivatives, N alpha- benzyloxycarbonylcitrulline p-nitroanilide, benzyloxycarbonylphenylalanylcitrulline p-nitroanilide and benzyloxycarbonylglycylphenylalanylcitrulline p-nitroanilide, were obtained. It is concluded that benzyloxycarbonylphenylalanylcitrulline p-nitroanilide is a highly selective substrate for the sensitive detection and assay of the plant cysteine proteinases.

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Year:  1984        PMID： 6721861      PMCID： PMC1153481          DOI： 10.1042/bj2190325

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  17 in total

1.  Mapping the active site of papain with the aid of peptide substrates and inhibitors.

Authors:  A Berger; I Schechter
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  1970-02-12       Impact factor: 6.237

2.  Chemical studies on methionyl-tRNA synthetase from Escherichia coli.

Authors:  C J Bruton; B S Hartley
Journal:  J Mol Biol       Date:  1970-09-14       Impact factor: 5.469

3.  Kinetics of papain-catalyzed hydrolysis of -N-benzoyl-L-arginine-p-nitroanilide.

Authors:  J E Mole; H R Horton
Journal:  Biochemistry       Date:  1973-02-27       Impact factor: 3.162

4.  Kinetic specificity in papain-catalysed hydrolyses.

Authors:  G Lowe; Y Yuthavong
Journal:  Biochem J       Date:  1971-08       Impact factor: 3.857

5.  On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain.

Authors:  I Schechter; A Berger
Journal:  Biochem Biophys Res Commun       Date:  1968-09-06       Impact factor: 3.575

6.  The preparation and properties of trans-cinnamoyl-papain.

Authors:  L J Brubacher; M L Bender
Journal:  J Am Chem Soc       Date:  1966-12-20       Impact factor: 15.419

7.  On the size of the active site in proteases. I. Papain.

Authors:  I Schechter; A Berger
Journal:  Biochem Biophys Res Commun       Date:  1967-04-20       Impact factor: 3.575

8.  Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for enzyme--leaving-group interaction.

Authors:  L Polgár
Journal:  Eur J Biochem       Date:  1979-08-01

9.  Kinetics of the hydrolysis of N-benzoyl-L-serine methyl ester catalysed by bromelain and by papain. Analysis of modifier mechanisms by lattice nomography, computational methods of parameter evaluation for substrate-activated catalyses and consequences of postulated non-productive binding in bromelain- and papain-catalysed hydrolyses.

Authors:  C W Wharton; A Cornish-Bowden; K Brocklehurst; E M Crook
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

10.  A new substrate for papain, benzoyl-L-arginine-p-nitroanilide (L-BAPA).

Authors:  S Tokura; N Nishi; J Noguchi
Journal:  J Biochem       Date:  1971-03       Impact factor: 3.387
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  2 in total

1.  Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides.

Authors:  E D Nery; M A Juliano; M Meldal; I Svendsen; J Scharfstein; A Walmsley; L Juliano
Journal:  Biochem J       Date:  1997-04-15       Impact factor: 3.857

2.  Chemical synthesis and papain-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitroanilide.

Authors:  N E Mackenzie; J P Malthouse; A I Scott
Journal:  Biochem J       Date:  1985-03-01       Impact factor: 3.857
  2 in total

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