Literature DB >> 421784

Determinant of efficiency of a monomeric enzyme: acceleration by site-specific molecules for trypsin.

K Tanizawa, Y Kanaoka.   

Abstract

The interaction of a specific ligand at substrate binding site was shown to be responsible for the catalytic efficiency of trypsin. The reasoning of 'induced fit' theory was refined by kinetic analysis of characteristic properties of 'inverse' substrates.

Mesh：

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Year:  1979        PMID： 421784     DOI： 10.1007/bf01917847

Source DB:  PubMed          Journal:  Experientia        ISSN： 0014-4754


  9 in total

1.  THE MECHANISM OF THE SPECIFICITY OF TRYPSIN CATALYSIS. 3. ACTIVATION OF THE CATALYTIC SITE OF TRYPSIN BY ALKYLAMMONIUM IONS IN THE HYDROLYSIS OF ACETYLGLYCINE ETHYL ESTER.

Authors:  T INAGAMI; T MURACHI
Journal:  J Biol Chem       Date:  1964-05       Impact factor: 5.157

2.  ON THE ACTIVATION OF TRYPSIN BY AMINES.

Authors:  B F ERLANGER; H CASTLEMAN
Journal:  Biochim Biophys Acta       Date:  1964-06-01

3.  Application of a Theory of Enzyme Specificity to Protein Synthesis.

Authors:  D E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  1958-02       Impact factor: 11.205

4.  "Inverse substrates" for trypsin. Efficient enzymatic hydrolysis of certain esters with a cationic center in the leaving group1.

Authors:  K Tanizawa; Y Kasaba; Y Kanaoka
Journal:  J Am Chem Soc       Date:  1977-06-22       Impact factor: 15.419

5.  On the specificity of tryptic catalysis.

Authors:  F Seydoux; J Yon
Journal:  Biochem Biophys Res Commun       Date:  1971-08-06       Impact factor: 3.575

6.  Amines as modifiers of the tryptic hydrolysis of neutral substrates.

Authors:  F Seydoux; G Coutouly; J Yon
Journal:  Biochemistry       Date:  1971-06-08       Impact factor: 3.162

7.  Trypsin substrates derived from benzamidine: application to active site titration and isolation of acyl-enzyme intermediate.

Authors:  K Tanizawa; S I Ishii; Y Kanaoka
Journal:  Biochem Biophys Res Commun       Date:  1968-09-06       Impact factor: 3.575

8.  The interaction of trypsin with neutral substrates and modifiers.

Authors:  B M Sanborn; G E Hein
Journal:  Biochemistry       Date:  1968-10       Impact factor: 3.162

9.  Proteolytic enzymes. VI. Aromatic amidines as competitive inhibitors of trypsin.

Authors:  K Tanizawa; S Ishii; K Hamaguchi; Y Kanaoka
Journal:  J Biochem       Date:  1971-05       Impact factor: 3.387
  9 in total

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