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Specificity in the hydrolysis of N-acyl-L-phenylalanine 4-nitroanilides by chymotrypsin

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Summary

The affinity of N-acyl-L-phenylalanine 4-nitroanilides for chymotrypsin is enhanced as the hydrophobicity of non-amino acid residues in the P2-position of the substrates increases, whereas kcat remains nearly constant. On the other hand, if alanine or leucine is in the P2-position kcat increases with decreasing KM.

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Authors and Affiliations

  1. Bereich Biochemie, Sektion Biowissenschaften der Karl-Marx-Universität, DDR-701, Leipzig

    H. -D. Jakubke, H. Däumer, A. Könnecke, P. Kuhl & J. Fischer

  2. Institut für Enzymologie und Technische Mikrobiologie, DDR-1017, Berlin, Germany

    H. -D. Jakubke, H. Däumer, A. Könnecke, P. Kuhl & J. Fischer

Authors
  1. H. -D. Jakubke
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  2. H. Däumer
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  3. A. Könnecke
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  4. P. Kuhl
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  5. J. Fischer
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Jakubke, H.D., Däumer, H., Könnecke, A. et al. Specificity in the hydrolysis of N-acyl-L-phenylalanine 4-nitroanilides by chymotrypsin. Experientia 36, 1039–1040 (1980). https://doi.org/10.1007/BF01965954

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  • DOI: https://doi.org/10.1007/BF01965954

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