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Tyr-Pro-Ala + H2O = Tyr-Pro + Ala
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-
Tyr-Pro-Phe + H2O = Tyr-Pro + Phe
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-
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O = Tyr-Pro + Phe-Pro-Gly-Pro-Ile
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Tyr-Pro-Trp-Phe-NH2 + H2O = Tyr-Pro + Trp-Phe-NH2
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human neuropeptide Y + H2O = Tyr-Pro + Ser-Lys-Pro-Asp-Asn-Pro-Gly
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human peptide YY + H2O = Tyr-Pro + Ile-Lys-Pro-Glu-Ala-Pro-Gly-
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Tyr-Pro-4-nitroanilide + H2O = Tyr-Pro + 4-nitroaniline
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Tyr-Pro-7-amido-4-methylcoumarin + H2O = Tyr-Pro + 7-amino-4-methylcoumarin
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Tyr-Pro-Phe-Pro-NH2 + H2O = Tyr-Pro + Phe-Pro-NH2
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Tyr-Pro-Phe-Val-Glu-Pro-Ile + H2O = Tyr-Pro + Phe-Val-Glu-Pro-Ile
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Tyr-Pro-7-amido-4-methylcoumarin + H2O = Tyr-Pro + 7-amino-4-methylcoumarin
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Tyr-Pro-Phe-Pro + H2O = Tyr-Pro + Phe-Pro
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-
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Prolidase from Xanthomonas maltophilia: purification and characterization of the enzyme
1995
Suga, K.; Kabashima, T.; Ito, K.; Tsuru, D.; Okamura, H.; Kataoka, J.; Yoshimoto, T.
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Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR
1992
Yan, T.R.; Ho, S.C.; Hou, C.L.
Biosci. Biotechnol. Biochem.
56
704-707
The unique properties of dipeptidyl-peptidase IV (DPP IV / CD26) and the therapeutic potential of DPP IV inhibitors
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Augustyns, K.; Bal, G.; Thonus, G.; Belyaev, A.; Zhang, X.M.; Bollaert, W.; Lambeir, A.M.; Durinx, C.; Goossens, F.; Haemers, A.
Curr. Med. Chem.
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Exploration of the active site of dipeptidyl peptidase IV from Porphyromonas gingivalis: comparison with the human enzyme
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Lambeir, A.M.; Rea, D.; Fulop, V.; Kumagai, Y.; Augustyns, K.; De Meester, I.; Haemers, A.; Scharpe, S.
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524
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Purification and characterization of barley dipeptidyl peptidase IV
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Davy, A.; Thomsen, K.K.; Juliano, M.A.; Alves, L.C.; Svendsen, I.; Simpson, D.J.
Plant Physiol.
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425-432
Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique
2007
Zhu, X.L.; Matsui, T.; Watanabe, K.; Shiraishi, K.; Ueki, T.; Matsumoto, K.
J. Agric. Food Chem.
55
8367-8371
Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases
2017
Are, V.N.; Kumar, A.; Kumar, S.; Goyal, V.D.; Ghosh, B.; Bhatnagar, D.; Jamdar, S.N.; Makde, R.D.
Biochim. Biophys. Acta
1865
153-164
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