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Anhydride Intermediates in Catalysis by Pepsin: Is Pepsin an Enzyme with Two Active Sites?

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Acid Proteases: Structure, Function, and Biology

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 95))

Abstract

Porcine pepsin is known to have two types of activities in acidic solution: the catalysis of peptide bond hydrolysis and the catalysis of transpeptidation (1). The presence of amino-enzyme intermediates in the catalytic action of pepsin has been proposed by Knowles (2–4) and Antonov et al. (5). On the other hand, Silver (6) and Hofmann (7) have proposed the existence of acyl-pepsin intermediates. Some mechanisms for pepsin action such as that suggested by Zeffren and Kaiser (8) involve the postulation of both acyl- and amino-enzyme intermediates. Recently, Fruton (9,10) has suggested that kinetically significant conformational changes of the pepsin active site in the presence of substrates or products instead of the formation of acyl-enzyme or amino-enzyme intermediates may account for the various data obtained for peptide hydrolysis and transpeptidation.

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Authors and Affiliations

  1. Departments of Chemistry and Biochemistry, University of Chicago, Chicago, Illinois, 60637, USA

    E. T. Kaiser & Y. Nakagawa

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  1. E. T. Kaiser
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  2. Y. Nakagawa
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  1. Oklahoma Medical Research Foundation, USA

    Jordan Tang

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© 1977 Springer Science+Business Media New York

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Kaiser, E.T., Nakagawa, Y. (1977). Anhydride Intermediates in Catalysis by Pepsin: Is Pepsin an Enzyme with Two Active Sites?. In: Tang, J. (eds) Acid Proteases: Structure, Function, and Biology. Advances in Experimental Medicine and Biology, vol 95. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0719-9_10

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  • DOI: https://doi.org/10.1007/978-1-4757-0719-9_10

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  • Publisher Name: Springer, New York, NY

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