Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
-
-
-
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic triad consists of Ser548-Asp631-His667
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship, the substrate induces an opening at the interface pf the peptidase and the beta-propeller domains while entering into the active site, concerted movements of the domains are required for enzyme activity
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic residues are Ser477, Asp559, and His591
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad is formed by conserved residues Ser548, Asp631, and His667
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser554, Asp641, His680 is located at the C-terminus in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance, catalytic mechanism, structure-function relationship, overview
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser554, Asp641, His680 is located at the C-terminus in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance, catalytic mechanism, structure-function relationship, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
18 kD protein of photosystem II + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
Products: -
?
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
Products: -
?
2-aminobenzoyl-EGPQGLLGA-3-nitrotyrosyl-NH2 + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-FFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-FP + Q-(N-(2,4-dinitrophenyl)ethylenediamine)
-
Substrates: -
Products: -
?
2-aminobenzoyl-FSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-Glu-Gly-L-Phe-Gly-L-Pro-L-Phe-Gly-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-Glu-Gly-L-Phe-Gly-L-Pro + L-Phe-Gly-L-4-nitrophenylalanine-L-Ala
-
Substrates: -
Products: -
?
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
Substrates: -
Products: -
?
2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Glu-Ser-Pro + Phe(NO2)-Arg-Ala
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-L-Phe-Gly-L-Pro-L-Phe-Gly-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-Gly-L-Phe-Gly-L-Pro + L-Phe-Gly-L-4-nitrophenylalanine-L-Ala
-
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-L-Phe-L-Arg-L-Pro-L-4-nitrophenylalanine-L-Arg-L-Ala + H2O
2-aminobenzoyl-Gly-L-Phe-L-Arg-L-Pro + L-4-nitrophenylalanine-L-Arg-L-Ala
-
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Arg-Pro + Phe(NO2)-Arg-Ala
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Glu-Pro + Phe(NO2)-Arg-Ala
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O
2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: a fluorescence resonance energy transfer peptide
Products: -
?
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
Products: -
?
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
Products: -
?
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Gln-N-(2,4-dinitrophenyl)ethylenediamine
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: a fluorescence resonance energy transfer peptide
Products: -
?
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: a fluorescence resonance energy transfer peptide
Products: -
?
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
Substrates: a fluorescence resonance energy transfer peptide
Products: -
?
2-aminobenzoyl-L-Ser-L-Pro-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-L-Ser-L-Pro + 4-nitrophenylalanine-L-Ala
-
Substrates: -
Products: -
?
2-aminobenzoyl-RPPGFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
Substrates: -
Products: -
?
2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-RPP + GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
Substrates: -
Products: -
?
2-aminobenzoyl-SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
Substrates: -
Products: -
?
4-((4-(dimethylamino)phenyl)azo)benzoyl-GPQGLLGA-L-glutamyl-gamma-(2-(1-sulfonyl-5-naphthyl)-aminoethylamide)-NH2 + H2O
?
-
Substrates: -
Products: -
?
Abz-Ala-Ala-Pro-4-nitrophenylalanine + H2O
Abz-Ala-Ala-Pro + 4-nitrophenylalanine
Abz-Ala-Pro-Ala-4-nitrophenylalanine + H2O
Abz-Ala-Pro + L-Ala-4-nitrophenylalanine
Abz-Ala-Pro-Gly-4-nitrophenylalanine + H2O
Abz-Ala-Pro + Gly-4-nitrophenylalanine
Abz-Gly-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Gly-Pro + 4-nitrophenylalanine
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala + H2O
Abz-Gly-L-Phe-L-Arg-L-Pro + L-Phe(NO2)-L-Arg-L-Ala
-
Substrates: -
Products: -
?
Abz-Gly-L-Phe-L-Ser-L-Pro-L-Phe-L-Arg-L-Ser-L-Ser-L-Arg-L-Ile-Gly-L-Glu-L-Ile-L-Lys-L-Glu-L-Glu-L-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
Abz-Gly-L-Phe-L-Ser-L-Pro + L-Phe-L-Arg-L-Ser-L-Ser-L-Arg-L-Ile-Gly-L-Glu-L-Ile-L-Lys-L-Glu-L-Glu-L-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
-
Substrates: -
Products: -
?
Abz-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Pro + 4-nitrophenylalanine
Abz-Lys-Pro-4-nitrophenylalanine + H2O
Abz-Lys-Pro + 4-nitrophenylalanine
AbzGFGPFGF(p-NO2)A-NH2 + H2O
AbzGFGP + FGF(p-NO2)A-NH2
-
Substrates: assay at pH 8.0, 37Ā°C, reaction stopped by heating at 95Ā°C for 5 min
Products: -
?
Ac-CDPGYIGSR-NH2 + H2O
?
-
Substrates: substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
Products: -
?
Ala-Ala-Pro-4-nitroanilide + H2O
Ala-Ala-Pro + 4-nitroaniline
-
Substrates: -
Products: -
?
Ala-Gly-Pro-beta-naphthylamide + H2O
Ala-Gly-Pro + 2-naphthylamine
Lyophyllum cinerascens
-
Substrates: -
Products: -
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
Substrates: -
Products: -
?
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
-
Substrates: -
Products: -
?
alpa2-antiplasmin + H2O
?
-
Substrates: not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
Products: -
?
alpha-melanocyte-stimulating hormone + H2O
?
alpha-melanocyte-stimulating hormone + H2O
acetyl-SYSMEHFRWGKP + L-Val
Substrates: acetyl-SYSMEHFRWGKPV
Products: -
?
alpha-MSH(1-13) + H2O
alpha-MSH(1-12) + Pro
-
Substrates: increased ratio between substrate and product in pituitaries of prolyl endopeptidase deficient mice compared to wild type mice
Products: -
?
alpha-synuclein + H2O
?
-
Substrates: -
Products: -
?
alpha-synulein + H2O
?
-
Substrates: the enzyme binds to alpha-synuclein and enhances its dimerization
Products: -
?
alpha2-gliadin 33-mer + H2O
?
-
Substrates: the enzyme is able to break down 63% of the 33-mer after 8 h of incubation and it is almost completely degraded after 12 h
Products: -
?
angiotensin I + H2O
DRVYIHP + FHL
Substrates: DRVYIHPFHL
Products: -
?
angiotensin II + H2O
DRVYIHP + L-Phe
Substrates: DRVYIHPF
Products: -
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
Substrates: -
Products: -
?
Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln + H2O
Arg-Pro-Lys-His-Pro + Ile-Lys-His-Gln
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
Substrates: -
Products: -
?
arginine-vasopressin + H2O
?
Asp-Pro-4-nitroanilide + H2O
Asp-Pro + 4-nitroaniline
-
Substrates: -
Products: -
?
Asp-Pro-p-nitroanilide + H2O
Asp-Pro + p-nitroaniline
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Ala-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + 4-nitroaniline
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Ala-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Ala + beta-naphthylamine
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Ala-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + p-nitroaniline
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Ala-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Ala + p-nitrophenol
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Gly-Pro + p-nitrophenol
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-Ala-Pro-2-naphthylamide + H2O
?
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + 4-nitroaniline
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Pro + beta-naphthylamine
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Ala-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + p-nitroaniline
benzyloxycarbonyl-Ala-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Pro + p-nitrophenol
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-D-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + p-nitrophenol
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Pro + beta-naphthylamine
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
benzyloxycarbonyl-Gly-L-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-L-Pro + 2-naphthylamine
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-L-Pro-beta-naphthylamide + H2O
?
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-L-Pro-doxorubicin + H2O
benzyloxycarbonyl-Gly-L-Pro + doxorubicin
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-L-Pro-melphalan + H2O
benzyloxycarbonyl-Gly-L-Pro + melphalan
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-2-beta-naphthylamide + H2O
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
benzyloxycarbonyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-Gly-Pro-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + D-Ala
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-Gly-Pro-D-Leu + H2O
benzyloxycarbonyl-Gly-Pro + D-Leu
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Ala
benzyloxycarbonyl-Gly-Pro-Leu-Gly-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-D-Ala
-
Substrates: enzyme from kidney
Products: -
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Gly
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
benzyloxycarbonyl-Gly-Pro-SBzl + H2O
benzyloxycarbonyl-Gly-Pro + phenyl-methanethiol
Substrates: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-thiobenzyl ester + H2O
benzyloxycarbonyl-Gly-Pro + phenylmethanethiol
-
Substrates: -
Products: -
?
benzyloxycarbonyl-glycyl-l-prolyl-4-nitroanilide + H2O
?
-
Substrates: -
Products: -
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
benzyloxycarbonyl-L-Ala-L-Ala-L-Pro p-nitroanilide + H2O
?
benzyloxycarbonyl-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Pro + p-nitrophenol
-
Substrates: enzyme from kidney
Products: -
?
beta-amyloid + H2O
?
-
Substrates: -
Products: -
?
beta-endorphin + h2O
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro + Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala + Ile-Ile-Lys-Asn-Ala + Tyr-Lys-Lys-Gly-Glu
Substrates: -
Products: -
?
bradykinin + H2O
Arg-Pro-Pro + Gly-Phe-Ser-Pro + Phe-Arg
show
top
