Heins J, Welker P, Schönlein C, Born I, Hartrodt B, Neubert K, Tsuru D, Barth A
Martin-Luther-University, Biotechnikum, Halle/S, D.D.R.
Biochim Biophys Acta. 1988 May 18;954(2):161-9. doi: 10.1016/0167-4838(88)90067-2.
The substrate specificity of dipeptidyl peptidase IV (dipeptidyl peptide hydrolase, EC 3.4.14.5) from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum, was investigated with a series of N-terminal unprotected (dipeptidyl peptidases IV) and succinylated dipeptidyl-p-nitroanilides (proline-specific endopeptidase). Both enzymes are specific for the S configuration of the amino-acid residue in P1 and P2 position if the penultimate residue is proline. In the case of alanine substrates (Ala in P1, dipeptidyl peptidase IV hydrolyzes such compounds where the configuration of the P2 residue is R. The penultimate residue with dipeptidyl peptidase IV can be, beside proline and alanine, dehydroproline, hydroxyproline and pipecolic acid. Proline substrates (Pro in P1) with an R configuration in P2 are inhibitors of the hydrolysis of proline substrates with an S,S configuration in an uncompetitive (dipeptidyl peptide IV) or mixed inhibition type (proline-specific endopeptidase). Derivatives of Gly-Pro-pNA where the N-terminal amino group is methylated are hydrolyzed by dipeptidyl peptidase IV.
利用一系列N端未保护的（二肽基肽酶IV）和琥珀酰化二肽基对硝基苯胺（脯氨酸特异性内肽酶），研究了猪肾二肽基肽酶IV（二肽基肽水解酶，EC 3.4.14.5）和脑膜败血黄杆菌脯氨酸特异性内肽酶的底物特异性。如果倒数第二个残基是脯氨酸，这两种酶对P1和P2位置氨基酸残基的S构型具有特异性。对于丙氨酸底物（P1为Ala），二肽基肽酶IV水解P2残基构型为R的此类化合物。除脯氨酸和丙氨酸外，二肽基肽酶IV的倒数第二个残基还可以是脱氢脯氨酸、羟脯氨酸和哌啶酸。P2构型为R的脯氨酸底物（P1为Pro）对P2构型为S,S的脯氨酸底物的水解具有非竞争性抑制作用（二肽基肽酶IV）或混合抑制作用（脯氨酸特异性内肽酶）。N端氨基甲基化的甘氨酰-脯氨酰-pNA衍生物可被二肽基肽酶IV水解。
