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- Title
Extended Investigation of the Substrate Specificity of Dipeptidyl Peptidase IV from Pig Kidney.
- Authors
RAHFELD5, Jens; SCHUTKOWSKI, Mike; FAUST, Jürgen; NEUBERT, Klaus; EARTH, Alfred; HEINS, Jochen
- Abstract
The substrate specificity of dipeptidyl peptidase IV(dipeptidyl peptide hydrolase, EC 3.4.14.5) from pig kidney was investigated, using a series of substrates, in which the amino-acid residue in position P1, a structural derivative of proline, was altered with respect to ring size and substituents. It was demonstrated that dipeptidyl peptidase IV hydrolyses substrates of the type Ala-X-pNA, where X is proline (Pro), (JR)-thiazolidine-4-carboxylic acid (Thz), (S)- pipecolic acid (Pip), (S)-oxazolidine-4-carboxylic acid (Oxa), or (S)-azetidine-2-carboxylic acid (Aze). The ring size and ring structure of the residue in the PI position influence the rate of enzyme-catalysed hydrolysis of the substrate. The highest kcat value (814 s-1) was found for Ala-Aze-pNA. In contrast, the Kcat value for Ala-Pro-pNA is nearly 55 s-1. With all substrates of this series, the rate-limiting step of the hydrolysis by dipeptidyl peptidase IV is the deacylation reaction. Compounds of substrate-like structure, in which the P2 residue has an R-configuration, are not hydrolysed by dipeptidyl peptidase IV.
- Publication
Biological Chemistry, 1991, Vol 372, Issue 1, p313
- ISSN
1431-6730
- Publication type
Article