Ligand benzyloxycarbonyl-Gly-Pro-p-nitrophenol
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Basic Ligand Information
Molecular Structure

C21H21N3O7
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
MAXYPAJZEQDQRB-SFHVURJKSA-N
benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester, benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester, N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester, N-benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (4 results)
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benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O = benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
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benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O = benzyloxycarbonyl-Gly-Pro + p-nitrophenol
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N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O = N-benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
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N-benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester + H2O = ?
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (5 results)
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0.021
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pH 7.0, mutant enzyme D641N
0.031
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pH 7.0, mutant enzyme D641A
3
6
pH 7.0, wild-type enzyme
32.7
-
enzyme from kidney
KM Value (6 results)
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0.000025
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pH 7.0, mutant enzyme D641A
0.000028
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pH 7.0, mutant enzyme D641N
0.0192
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pH 7.0, wild-type enzyme
0.07
-
enzyme from kidney
References & Links
Literature References (5)
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Proline-specific endopeptidase from Flavobacterium. Purification and properties
1980
Yoshimoto, T.; Walter, R.; Tsuru, D.
J. Biol. Chem.
255
4786-4792
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase
2002
Szeltner, Z.; Rea, D.; Juhasz, T.; Renner, V.; Mucsi, Z.; Orosz, G.; Fulop, V.; Polgar, L.
J. Biol. Chem.
277
44597-44605
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Proline-specific endopeptidases
2003
Besedin, D.V.; Rudenskaya, G.N.
Russ. J. Bioorg. Chem.
29
1-17
Truncated prolyl oligopeptidase from Pyrococcus furiosus
2007
Juhasz, T.; Szeltner, Z.; Polgar, L.
Proteins
69
633-643
Ligand-induced conformational changes in prolyl oligopeptidase A kinetic approach
2017
Van Elzen, R.; Schoenmakers, E.; Brandt, I.; Van Der Veken, P.; Lambeir, A.
Protein Eng. Des. Sel.
30
219-226
Links to other databases for benzyloxycarbonyl-Gly-Pro-p-nitrophenol