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• W2077978055 abstract "Proline-containing dipeptidyl-4-nitroanilides have been synthesised and subjected to dipeptidyl peptidase IV-catalysed hydrolysis at high enzyme concentrations to collect information on the conformational specificity of the enzyme active site for a nonscissile bond. Descriptions of the biphasic kinetics were carried out in terms of cis/trans interconversion of the substrates. The results show that the enzyme can cleave only the trans-conformation of the substrate. The competitive inhibition by Gly-Pro-OH and Ala-Pro-OH is also specific for the trans form of the dipeptides. The interpretation of the results obtained from these kinetic studies has led to proposals for the stepwise cleavage of biologically active peptides like substance P and beta-casomorphine by dipeptidyl peptidase IV." @default.
• W2077978055 created "2016-06-24" @default.
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• W2077978055 creator A5058816586 @default.
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• W2077978055 date "1983-02-01" @default.
• W2077978055 modified "2023-10-17" @default.
• W2077978055 title "The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases" @default.
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• W2077978055 doi "https://doi.org/10.1016/0167-4838(83)90261-3" @default.
• W2077978055 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6340741" @default.
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