Kinetics of Hydrolysis of a New Peptide Substrate Containing p-Guanidino-L-phenylalanine by Trypsin and Thrombin
A new peptide substrate containing p-guanidine-L-phenylalanine, Nα-benzoyl-L-phenylalanyl-L-prolyl-p-guanidino-L-phenylalanine p-nitroanilide (Bz-Phe-Pro-GPA-pNA), was synthesized, and the rates of hydrolyses of this substrate by bovine trypsin and thrombin were compared with those of the correspond...
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Veröffentlicht in: | Chemical & pharmaceutical bulletin 1986/03/25, Vol.34(3), pp.1351-1354 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A new peptide substrate containing p-guanidine-L-phenylalanine, Nα-benzoyl-L-phenylalanyl-L-prolyl-p-guanidino-L-phenylalanine p-nitroanilide (Bz-Phe-Pro-GPA-pNA), was synthesized, and the rates of hydrolyses of this substrate by bovine trypsin and thrombin were compared with those of the corresponding arginine peptide substrate (Bz-Phe-Pro-GPA-pNA). The specificity constants (kcat/Km) for the hydrolysis of GPA-peptide by the two enzymes were much smaller than those for Arg-peptide. Remarkably low kcat values were found in the hydrolyses of GPA-peptide by the two enzymes compared with the values in those of Arg-peptide. The effect of the peptide chain elongation was observed in the hydrolysis of GPA-peptide by thrombin, while it was not in the case of trypsin, suggesting that the subsite of trypsin is very different from that of thrombin. GPA-peptide was ascertained to be a useful peptide substrate to study the subsite specificities of trypsin-like enzymes. |
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ISSN: | 0009-2363 1347-5223 |
DOI: | 10.1248/cpb.34.1351 |