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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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Prolidase from Xanthomonas maltophilia: purification and characterization of the enzyme
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Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases
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Are, V.N.; Kumar, A.; Kumar, S.; Goyal, V.D.; Ghosh, B.; Bhatnagar, D.; Jamdar, S.N.; Makde, R.D.
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