Weidhase, R. and Welker, P. and Neubert, K. and Dove, Stefan and Yoshimoto, T. and Tsuru, D. and Barth, A. (1984) Similarities of the substrate cleavage catalyzed by proline specific endopeptidase and dipeptidyl peptidase IV. Pharmazie 39 (12), pp. 835-837.
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Sixteen substrates of the type succinyl-Ala-Ala-pX-anilide and succinyl-Ala-Pro-pX anilide having different substituents (X) in p-position of the aryl residue were synthesized and characterized. The influence of electronic as well as hydrophobic substituent consts., s and p, on the hydrolysis of substrates catalyzed by proline-specific endopeptidase (PSE) was investigated. In the Hansch approach, the catalytic consts. log kcat and log (kcat/Km) of succinyl-Ala-Ala-pX-anilides hydrolyzed by PSE correlate significantly with electronic substituent consts. s, whereas there is no correlation in the case of succinyl-Ala-Pro-pX-anilides. The intercorrelation data from dipeptidyl peptidase IV-catalyzed hydrolysis of Ala-Ala-pX-anilides suggest that both enzymes act by a similar catalytic mechanism.
|Institutions:||Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)|
|Subjects:||500 Science > 540 Chemistry & allied sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||No|
|Owner:||Prof. Dr. Stefan Dove|
|Deposited On:||14 Jan 2009 16:12|
|Last Modified:||05 Aug 2009 15:50|
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