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release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
-
-
-
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic mechanism, Asp160, Met161, Gly201, Arg202, and Phe219 are involved, active site structure, modeling of enzyme-substrate complex
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic mechanism, high preference towards large hydrophobic amino terminus residues, active site structure, Glu131 is involved in the catalytic mechanism, enzyme-substrate and enzyme-product complex modeling
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
hydrolyses peptide bonds formed by terminal hydrophobic amino acids such as leucine, methionine, and phenylalanine
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
M161 is involved in substrate binding at the active site cleft
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
preference for hydrophobic residues at the ultimate and the penultimate positions, D-amino acids at these positions reduce the activity, activity is not restricted by the length of substrate chains
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic pathway and reaction mechanism, catalytic residues are Glu131 and Tyr246, Tyr246 is involved in stabilization of the reaction transition state intermediate, also residue Glu151 is involved
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
raction mechanism, catalytic residues are Glu131 and Tyr246, residues Arg202 and Asp160 stabilize the reaction intermediate together with Glu131
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
structure and reaction mechanism
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
the enzyme prefers large hydrophobic aminoterminal residues, Glu131, Asp160, and Arg202 are involved in binding of the N-terminal substrate amino acid, substrate binding and reaction mechanism, tetrahedral reaction intermediate, modelling of the enzyme-substrate and enzyme-product complexes
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic reaction mechanism, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5, involvement of a zinc-bound hydroxide as the reaction nucleophile, Tyr246 polarizes the carbonyl carbon and stabilizes the transition state, enzyme-substrate interaction, overview
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
structure and reaction mechanism
-
-
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4-nitrophenyl phenylphosphonate + H2O
4-nitrophenol + phenylphosphonate
-
-
-
-
?
4-nitrophenyl-L-leucine + H2O
4-nitrophenol + L-leucine
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-OBzl + benzyl alcohol
bis(4-nitrophenyl) phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
bis(4-nitrophenyl) phosphate + H2O
?
-
assay at pH 8.0, 30°C
-
-
?
bis(p-nitrophenyl)phosphate + H2O
?
-
-
-
?
D-Arg-OMe + L-Pro-OBzl
c(L-Pro-D-Arg) + benzyl alcohol + methanol
-
-
-
-
?
D-Arg-OMe + L-Pro-OBzl
L-Pro-D-Arg-OMe + benzyl alcohol
-
-
-
-
?
D-Leu-OBzl + D-Leu-OBzl
D-Leu-D-Leu-OBzl + benzyl alcohol
-
-
-
-
?
D-Leu-OMe + D-Leu-OMe
D-Leu-D-Leu-OMe + methanol
-
-
-
-
?
D-Leu-OMe + D-Pro-OBzl
D-Pro-D-Leu-OMe + benzyl alcohol
-
-
-
-
?
D-Leu-OMe + L-Pro-OBzl
L-Pro-D-Leu-OMe + benzyl alcohol
-
-
-
-
?
D-Phe-OMe + D-Pro-OBzl
D-Pro-D-Phe-OMe + benzyl alcohol
-
-
-
-
?
D-Phe-OMe + L-Pro-OBzl
L-Pro-D-Phe-OMe + benzyl alcohol
-
-
-
-
?
D-Trp-OMe + D-Pro-OBzl
D-Pro-D-Trp-OMe + benzyl alcohol
-
-
-
-
?
D-Trp-OMe + L-Pro-OBzl
L-Pro-D-Trp-OMe + benzyl alcohol
-
-
-
-
?
D-Tyr-OMe + D-Pro-OBzl
D-Pro-D-Tyr-OMe + benzyl alcohol
-
-
-
-
?
D-Tyr-OMe + L-Pro-OBzl
L-Pro-D-Tyr-OMe + benzyl alcohol
-
-
-
-
?
D-Val-OBzl + D-Val-OBzl
D-Val-D-Val-OBzl + benzyl alcohol
-
-
-
-
?
D-Val-OMe + L-Pro-OBzl
L-Pro-D-Val-OMe + benzyl alcohol
-
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
5.4% of the activity with Lys-4-nitroanilide
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
?
Gly-Leu-Gly + H2O
?
-
-
-
?
human hemoglobin alpha-chain + H2O
?
-
hydrolysis of the first few residues to proline at the 4th position
-
?
human hemoglobin beta-chain + H2O
?
-
hydrolysis of the first few residues to proline at the 5th position
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
L-Ala-OMe + L-Pro-OBzl
L-Pro-L-Ala-OMe + benzyl alcohol
-
-
-
-
?
L-alanine-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
L-alanine-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
L-Arg-OMe + beta-Ala-OBzl
beta-Ala-L-Arg-OMe + benzyl alcohol
L-Arg-OMe + L-Pro-OBzl
c(L-Pro-L-Arg) + benzyl alcohol + methanol
-
-
-
-
?
L-Arg-OMe + L-Pro-OBzl
L-Pro-L-Arg-OMe + benzyl alcohol
-
-
-
-
?
L-Asn-OMe + beta-Ala-OBzl
beta-Ala-L-Asn-OMe + benzyl alcohol
L-Asp-OMe + L-Pro-OBzl
L-Pro-L-Asp-OMe + benzyl alcohol
-
-
-
-
?
L-Glu-OMe + L-Pro-OBzl
L-Pro-L-Glu-OMe + benzyl alcohol
-
-
-
-
?
L-His-OMe + beta-Ala-OBzl
beta-Ala-L-His-OMe + benzyl alcohol
L-His-OMe + D-Pro-OBzl
c(D-Pro-L-His) + benzyl alcohol + methanol
-
-
-
-
?
L-His-OMe + D-Pro-OBzl
D-Pro-L-His-OMe + benzyl alcohol
-
-
-
-
?
L-His-OMe + L-Pro-OBzl
c(L-Pro-L-His) + benzyl alcohol + methanol
-
-
-
-
?
L-His-OMe + L-Pro-OBzl
L-Pro-L-His-OMe + benzyl alcohol
-
-
-
-
?
L-Ile-OMe + beta-Ala-OBzl
beta-Ala-L-Ile-OMe + benzyl alcohol
L-Ile-OMe + D-Pro-OBzl
D-Pro-L-Ile-OMe + benzyl alcohol
-
-
-
-
?
L-Ile-OMe + L-Pro-OBzl
L-Pro-L-Ile-OMe + benzyl alcohol
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-Leu-NH2 + H2O
L-Leu + NH3
L-Leu-O-methyl ester + H2O
L-Leu + methanol
L-Leu-OEt + beta-Ala-OBzl
beta-Ala-L-Leu-OEt + benzyl alcohol
-
-
-
-
?
L-Leu-OEt + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Leu-beta-Ala-OBzl + benzyl alcohol + ethanol
-
-
-
-
?
L-Leu-OEt + D-Pro-OBzl
D-Pro-L-Leu-OEt + benzyl alcohol
-
-
-
-
?
L-Leu-OEt + L-Pro-OBzl
L-Pro-L-Leu-OEt + benzyl alcohol
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
L-Lys-OMe + beta-Ala-OBzl
beta-Ala-L-Lys-OMe + benzyl alcohol
-
-
-
-
?
L-Lys-OMe + L-Pro-OBzl
L-Pro-L-Lys-OMe + benzyl alcohol
-
-
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
good substrate
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
L-Met-OMe + beta-Ala-OBzl
beta-Ala-L-Met-OMe + benzyl alcohol
-
-
-
-
?
L-Met-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Met-OMe + benzyl alcohol
-
-
-
-
?
L-Met-OMe + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Met-beta-Ala-OBzl + benzyl alcohol + methanol
-
-
-
-
?
L-Met-OMe + D-Pro-OBzl
D-Pro-L-Met-OMe + benzyl alcohol
-
-
-
-
?
L-Met-OMe + L-Met-OMe + beta-Ala-OBzl
beta-Ala-L-Met-L-Met-OMe + benzyl alcohol + methanol
-
-
-
-
?
L-Met-OMe + L-Pro-OBzl
L-Pro-L-Met-OMe + benzyl alcohol
-
-
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
very good substrate
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
L-Phe-NH2 + H2O
L-Phe + NH3
-
-
-
?
L-Phe-O-methyl ester + H2O
L-Phe + methanol
-
-
-
?
L-Phe-OEt + beta-Ala-OBzl
beta-Ala-L-Phe-OEt + benzyl alcohol
-
-
-
-
?
L-Phe-OEt + beta-Ala-OBzl + beta-Ala-OBzl
beta-Ala-L-Phe-beta-Ala-OBzl + benzyl alcohol + ethanol
-
-
-
-
?
L-Phe-OEt + D-Pro-OBzl
D-Pro-L-Phe-OEt + benzyl alcohol
-
-
-
-
?
L-Phe-OEt + L-Phe-OEt + beta-Ala-OBzl
beta-Ala-L-Phe-L-Phe-OMe + benzyl alcohol + ethanol
-
-
-
-
?
L-Phe-OEt + L-Pro-OBzl
L-Pro-L-Phe-OEt + benzyl alcohol
-
-
-
-
?
L-phenylalanine ethyl ester + L-phenylalanine + H2O
L-Phe-L-Phe + cyclo(L-phenylalanine-L-phenylalanine) + L-Phe-L-Phe ethyl ester
L-phenylalanine-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
very good substrate
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
very low activity
-
-
?
L-Pro-OMe + beta-Ala-OBzl
L-Pro-beta-Ala-OBzl + methanol
-
-
-
-
?
L-Pro-OMe + beta-Ala-OBzl + beta-Ala-OBzl
L-Pro-(beta-Ala)2-OBzl + methanol + benzyl alcohol
-
-
-
-
?
L-proline-4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
good substrate
-
?
L-proline-p-nitroanilide + H2O
L-Pro + 4-nitroaniline
L-Ser-OMe + L-Pro-OBzl
L-Pro-L-Ser-OMe + benzyl alcohol
-
-
-
-
?
L-Thr-OMe + beta-Ala-OBzl
beta-Ala-L-Thr-OMe + benzyl alcohol
-
-
-
-
?
L-Thr-OMe + L-Pro-OBzl
L-Pro-L-Thr-OMe + benzyl alcohol
-
-
-
-
?
L-Thr-OMe + L-Thr-OMe
(L-Thr)2-OMe + methanol
-
-
-
-
?
L-Thr-OMe + L-Thr-OMe
L-Thr-L-Thr-OMe + methanol
-
-
-
-
?
L-Trp-OMe + beta-Ala-OBzl
beta-Ala-L-Trp-OMe + benzyl alcohol
-
-
-
-
?
L-Trp-OMe + D-Pro-OBzl
D-Pro-L-Trp-OMe + benzyl alcohol
-
-
-
-
?
L-Trp-OMe + L-Pro-OBzl
L-Pro-L-Trp-OMe + benzyl alcohol
-
-
-
-
?
L-Tyr-OMe + beta-Ala-OBzl
beta-Ala-L-Tyr-OMe + benzyl alcohol
-
-
-
-
?
L-Tyr-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Tyr-OMe + benzyl alcohol
-
-
-
-
?
L-Tyr-OMe + D-Pro-OBzl
D-Pro-L-Tyr-OMe + benzyl alcohol
-
-
-
-
?
L-Tyr-OMe + L-Pro-OBzl
L-Pro-L-Tyr-OMe + benzyl alcohol
-
-
-
-
?
L-Tyr-OMe + L-Tyr-OMe + beta-Ala-OBzl
beta-Ala-L-Tyr-L-Tyr-OMe + benzyl alcohol + methanol
-
-
-
-
?
L-Val-OBzl + L-Val-OBzl
L-Val-L-Val-OBzl + benzyl alcohol
-
-
-
-
?
L-Val-OMe + beta-Ala-OBzl
beta-Ala-L-Val-OMe + benzyl alcohol
-
-
-
-
?
L-Val-OMe + beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-L-Val-OMe + benzyl alcohol
-
-
-
-
?
L-Val-OMe + D-Pro-OBzl
D-Pro-L-Val-OMe + benzyl alcohol
-
-
-
-
?
L-Val-OMe + L-Pro-OBzl
L-Pro-L-Val-OMe + benzyl alcohol
-
-
-
-
?
L-valine-4-nitroanilide + H2O
L-valine + 4-nitroaniline
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
11.7% of the activity with Lys-4-nitroanilide
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
-
-
-
?
additional information
?
-
4-nitrophenyl-L-leucine + H2O
4-nitrophenol + L-leucine
-
-
-
-
?
4-nitrophenyl-L-leucine + H2O
4-nitrophenol + L-leucine
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
105.2% of the activity with Lys-4-nitroanilide
-
-
?
beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-OBzl + benzyl alcohol
-
-
-
-
?
beta-Ala-OBzl + beta-Ala-OBzl
(beta-Ala)2-OBzl + benzyl alcohol
-
-
-
-
?
Hemoglobin + H2O
?
-
human hemoglobin
-
-
?
Hemoglobin + H2O
?
-
human hemoglobin
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
very low activity
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
very low activity
-
-
?
L-alanine-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
-
?
L-alanine-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
-
?
L-alanine-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
L-alanine-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
good substrate
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
low activity
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
low activity
-
-
?
L-Arg-OMe + beta-Ala-OBzl
beta-Ala-L-Arg-OMe + benzyl alcohol
-
-
-
-
?
L-Arg-OMe + beta-Ala-OBzl
beta-Ala-L-Arg-OMe + benzyl alcohol
-
-
-
-
?
L-Asn-OMe + beta-Ala-OBzl
beta-Ala-L-Asn-OMe + benzyl alcohol
-
-
-
-
?
L-Asn-OMe + beta-Ala-OBzl
beta-Ala-L-Asn-OMe + benzyl alcohol
-
-
-
-
?
L-His-OMe + beta-Ala-OBzl
beta-Ala-L-His-OMe + benzyl alcohol
-
-
-
-
?
L-His-OMe + beta-Ala-OBzl
beta-Ala-L-His-OMe + benzyl alcohol
-
-
-
-
?
L-Ile-OMe + beta-Ala-OBzl
beta-Ala-L-Ile-OMe + benzyl alcohol
-
-
-
-
?
L-Ile-OMe + beta-Ala-OBzl
beta-Ala-L-Ile-OMe + benzyl alcohol
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
preferred substrate of the wild-type enzyme
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
preferred substrate of the wild-type enzyme
-
-
?
L-Leu-NH2 + H2O
L-Leu + NH3
-
-
-
?
L-Leu-NH2 + H2O
L-Leu + NH3
-
-
-
?
L-Leu-O-methyl ester + H2O
L-Leu + methanol
-
-
-
?
L-Leu-O-methyl ester + H2O
L-Leu + methanol
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
best of the amino acid 4-nitroanilide substrates
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
best of the amino acid 4-nitroanilide substrates
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
low activity
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
low activity
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
low activity
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
low activity
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
low activity
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
low activity
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
low activity
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
?
L-phenylalanine ethyl ester + L-phenylalanine + H2O
L-Phe-L-Phe + cyclo(L-phenylalanine-L-phenylalanine) + L-Phe-L-Phe ethyl ester
-
assay at 50°C
-
-
?
L-phenylalanine ethyl ester + L-phenylalanine + H2O
L-Phe-L-Phe + cyclo(L-phenylalanine-L-phenylalanine) + L-Phe-L-Phe ethyl ester
-
assay at 50°C
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
-
?
L-proline-p-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-proline-p-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-valine-4-nitroanilide + H2O
L-valine + 4-nitroaniline
-
-
-
?
L-valine-4-nitroanilide + H2O
L-valine + 4-nitroaniline
-
good substrate
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
12.2% of the activity with Lys-4-nitroanilide
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
assay at pH 8.0, 30°C
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Met-enkephalin + H2O
?
-
substrate is a pentapeptide with sequence Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus
-
-
?
Met-enkephalin + H2O
?
-
substrate is a pentapeptide with sequence Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus
-
-
?
peptide + H2O
?
-
-
?
peptide + H2O
?
-
substrate specificity
-
?
peptide + H2O
?
-
high preference towards large hydrophobic amino terminus residues
-
?
additional information
?
-
-
no activity with Gly-Pro-4-nitroanilide and Ala-Pro-4-nitroanilide, no acitivity with Xaa-Pro N-terminal sequences, glycine-4-nitroanilide and acidic amino acid 4-nitroanilide are very poor substrates
-
?
additional information
?
-
-
substrates with blocked amino groups are partially hydrolyzed, poor activity with Val-Gly, Val-Leu, and Trp-Leu, Gly-Gly-Gly and D-leucine-D-leucine are no substrates
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
no activity with L-Glu-4-nitroanilide, L-Arg-4-nitroanilide, D-Phe-4-nitroanilide, and D-Leu-4-nitroanilide, L-Ala-4-nitroanilide and L-Pro-4-nitroanilide are poor substrates
-
-
?
additional information
?
-
-
the enzyme is active on a wide variety of peptides substrates, no activity with D-Leu-D-Leu, no prolidase activity, but release of N-terminal prolyl residues
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position
-
-
?
additional information
?
-
the enzyme is active toward various peptides with different N-terminal side chains and specific toward hydrophobic ones, the enzyme also exhibits a significant activity toward the hydrolysis of the phosphodiester bis(p-nitrophenyl)phosphate, overview, active site structure involves the three auxiliary amino acid side chains of Tyr246, Glu131, and Arg202 that are involved in catalysis, modeling of substrate binding using the crystal structure of the enzyme, overview, the activity shows proton inventory and viscosity dependence, overview
-
-
?
additional information
?
-
-
the enzyme is active toward various peptides with different N-terminal side chains and specific toward hydrophobic ones, the enzyme also exhibits a significant activity toward the hydrolysis of the phosphodiester bis(p-nitrophenyl)phosphate, overview, active site structure involves the three auxiliary amino acid side chains of Tyr246, Glu131, and Arg202 that are involved in catalysis, modeling of substrate binding using the crystal structure of the enzyme, overview, the activity shows proton inventory and viscosity dependence, overview
-
-
?
additional information
?
-
-
the thermostable enzyme prefers large hydrophobic N-terminal residues in its peptide and protein substrates, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5
-
-
?
additional information
?
-
-
the enzyme is active on a wide variety of peptides substrates, no activity with D-Leu-D-Leu, no prolidase activity, but release of N-terminal prolyl residues
-
-
?
additional information
?
-
no activity with L-Glu-4-nitroanilide, D-Phe-4-nitroanilide, and D-Leu-4-nitroanilide
-
-
?
additional information
?
-
substrate specificities of recombinant wild-type and F221 mutant enzymes, overview
-
-
?
additional information
?
-
no activity with L-Glu-4-nitroanilide, D-Phe-4-nitroanilide, and D-Leu-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with L-Glu-4-nitroanilide, D-Phe-4-nitroanilide, and D-Leu-4-nitroanilide
-
-
?
additional information
?
-
substrate specificities of recombinant wild-type and F221 mutant enzymes, overview
-
-
?
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Mn2+
-
dinuclear metal-enzyme derivative, structure
Ni2+
-
dinuclear metal-enzyme derivative, structure
Ca2+
-
-
Ca2+
activates about 6fold, non-cooperative binding
Ca2+
-
activates, binds to the enzyme, activation level with different enzyme substrates, overview
Ca2+
-
activates, enhances stability of the enzyme, modulates the enzyme activity and affinity towards substrates and inhibitors in a structure-dependent manner, binding structure
Ca2+
-
location of binding site is in about 25 A distance from the zinc binding site, determination of structural environment
Ca2+
activates and stabilizes, influences substrate specificity, Asp173 and Asp174 are key residues in Ca2+ binding and important for enzyme activity, residues Asp3, Ile4, Asp262, and Asp266 are also involved in calcium binding but are important for enzyme stabilization, overview, binding capacity of recombinant wild-type and mutant enzymes, overview
Ca2+
-
activates the enzyme with some substrates, about 3fold with L-Leu-4-nitroanilide, and affects substrate specificity, e.g. decreases the activity with Lys-4-nitroanilide
Ca2+
-
activates, has complex effects on the enzyme, stabilizes the enzyme
Ca2+
-
affects metal binding, inhibition, and entropy of activation of the enzyme
Ca2+
modulating the enzyme activity
Cd2+
-
metal binding modelling using titration, kinetic, and thermodynamic data, dinuclear metal enzyme, sequential binding to two metal binding sites, affected by Ca2+
Cd2+
-
dinuclear metal-enzyme derivative, structure
Co2+
-
activity is strictly dependent on, maximal activity at 0.5 mM CoCl2
Co2+
-
metalloenzyme containing Co2+ in its structure
Co2+
-
the enzyme contains two metal ions with high occupancy and a third metal ion with low occupancy at the active site of the enzyme molecule, Glu319 and a water molecule are bridging, Glu253, His348, His381, Tyr355, and Asp383 are involved in metal binding, structure analysis
Co2+
-
slightly activating at 0.1-1 mM
Co2+
-
dinuclear metal-enzyme derivative, structure
Zn2+
-
the enzyme contains two metal ions with high occupancy and a third metal ion with low occupancy at the active site of the enzyme molecule, Glu319 and a water molecule are bridging, Glu253, His348, His381, Tyr355, and Asp383 are involved in metal binding, structure analysis
Zn2+
2 mol zinc per mol of enzyme, binding structure
Zn2+
-
2 mol zinc per mol of enzyme, binding structure
Zn2+
-
2 mol zinc per mol of enzyme, tightly bound at the active site in a distance of 3.6 A of each other, determination of structural environment
Zn2+
2 mol/mol of protein, tightly bound, zinc coordination amino acid residues are conserved in similar enzymes
Zn2+
-
double-zinc exopeptidase
Zn2+
-
metalloprotease, dependent on
Zn2+
metalloprotease, dependent on
Zn2+
-
zinc-metallo-exoprotease
Zn2+
-
the enzyme is a double-zinc aminopeptidase
Zn2+
the enzyme is a double-zinc aminopeptidase, metal ions are bound at the active site
Zn2+
-
the enzyme is a double-zinc aminopeptidase, the metal ions are bound at the active site, binding structure analysis
Zn2+
the enzyme is a double-zinc exopeptidase, binding structure, overview
Zn2+
-
the enzyme is a zinc-metalloenzyme containing 2 mol zinc per mol of enzyme, stabilizes the enzyme
Zn2+
-
double-zinc aminopeptidase
additional information
-
determination of metal ion identity
additional information
-
substitution of the Zn2+ ion by Mn2+ or Co2+ results in altered substrate specificity, e.g. the Co2+ containing enzyme highly prefers L-alanine-4-nitroanilide
additional information
-
the enzyme depends on metals
additional information
Ca2+ and Co2+ do not affect the enzyme's substrate specificity at 0.1-1 mM
additional information
-
the enzyme possesses dinuclear metal cluster
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-iodo-L-phenylalanine
-
weak inhibition, binds at the active site via the two zinc ions displacing the metal ions, binding structure analysis
antipain
-
0.01 mg/ml, 93% inhibition
bis(p-nitrophenyl)phosphate
-
Chloroquine
-
5 mM, 79% inhibition
CrCl2
-
1 mM, 83% inhibition in presence of 1 mM CoCl2
CuCl2
-
1 mM, 96% inhibition in presence of 1 mM CoCl2
diisopropylphosphofluoridate
-
pretreatment, complete inhibition
EGTA
complete inhibition, activity can be completely restored by addition of 1 mM CaCl2
free amino acids
-
competitive inhibition, highest inhibition by L-histidine
-
HgCl2
-
5 mM, 98% inhibition in presence of 1 mM CoCl2
L-leucine chloromethyl ketone
-
-
L-phenylalanine chloromethyl ketone
-
-
L-tryptophan
-
weak inhibition, binds at the active site via the two zinc ions displacing the metal ions, binding structure analysis
Leu-hydroxamate
-
1 mM, 73% inhibition
leupeptin
-
0.01 mg/ml, 51% inhibition
methionine
weak inhibitor, binding structure, overview
MgSO4
-
1 mM, 24% inhibition in presence of 1 mM CoCl2
MnSO4
-
1 mM, 26% inhibition in presence of 1 mM CoCl2
NiSO4
-
1 mM, 40% inhibition in presence of 1 mM CoCl2
nitrilotriacetic acid
-
5 mM, 95% inhibition
p-hydroxymercuribenzoate
-
5 mM, 90% inhibition
phenylalanine
weak inhibitor, binding structure, overview
phenylmethylsulfonyl fluoride
-
1 mM, 95% inhibition
PMSF
-
1 mM, complete inhibition
tosyl-lysine chloromethyl ketone
ZnCl2
-
1 mM, 70% inhibition in presence of 1 mM CoCl2
1,10-phenanthroline
-
1 mM, complete inhibition
1,10-phenanthroline
-
1 mM, 91% inhibition
1,10-phenanthroline
50% inhibition at pI 4.9
amastatin
-
-
bestatin
-
0.004 mg/ml, complete inhibition
bestatin
-
0.004 mg/ml, 94% inhibition
Ca2+
-
-
Ca2+
slight inhibition at 1 mM
Cd2+
-
-
Cu2+
-
-
EDTA
-
5 mM, 90% inhibition
EDTA
complete inhibition, activity cannot be completely restored by addition of 1 mM CaCl2 alone but together with 0.0001 mM ZnCl2 by 90%
EDTA
-
complete inhibition at 10 mM, reactivation by divalent metal ions
Fe2+
-
-
fluoride
uncompetitive inhibitor toward peptide hydrolysis
fluoride
-
noncompetitive inhibitor at pH 5.9-8.0, fluoride ion interacts equally with the free enzyme as with the enzyme-substrate complex
L-leucine
-
-
L-leucine
-
binding mechanism and structure
L-leucine
-
very low product inhibition
L-methionine
-
-
L-methionine
-
binding mechanism and structure
L-phenylalanine
-
-
L-phenylalanine
-
binding mechanism and structure
leucine
weak inhibitor, binding structure, overview
leucine
product inhibition occurs in peptide hydrolysis
Lys-hydroxamate
-
1 mM, 80% inhibition
Lys-hydroxamate
-
1 mM, 81% inhibition
Mg2+
-
-
Mg2+
slight inhibition at 0.1-1 mM
Mn2+
-
-
Ni2+
-
-
phosphate
noncompetitive inhibitor with peptide substrates, the enzyme-substrate-inhibitor ternary complex is inactive, but phosphate is a competitive inhibitor toward bis(p-nitrophenyl)phosphate hydrolysis, with Ki ranging from 2.31 to 315 mM at pH 5.0-9.0
tosyl-lysine chloromethyl ketone
-
2 mM, 80% inhibition
tosyl-lysine chloromethyl ketone
-
5 mM, 94% inhibition
Zn2+
-
-
additional information
-
the enzyme activity is completely abolished by metal chelating agents, but can be restored by addition of zinc or cobalt
-
additional information
-
nonchelating 1,7-phenanthroline has little effect on the activity
-
additional information
very low product inhibition by L-leucine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.4 - 14.9
4-nitrophenyl phenylphosphonate
7.8
Ala-4-nitroanilide
pH 8.0, 30°C
3.8 - 12.8
bis(4-nitrophenyl) phosphate
3.4
bis(p-nitrophenyl)phosphate
pH 8.0, 30°C
1.4
Gly-4-nitroanilide
pH 8.0, 30°C
4.08
L-Ala-4-nitroanilide
-
pH 8.0, 30°C
3.84 - 4.81
L-alanine-4-nitroanilide
0.25 - 4.07
L-Leu-4-nitroanilide
15.8 - 16.1
L-Leu-O-methyl ester
0.55 - 2.97
L-leucine-4-nitroanilide
0.34 - 1.85
L-Phe-4-nitroanilide
6.9 - 12.8
L-Phe-O-methyl ester
0.53
L-Val-4-nitroanilide
-
pH 8.0, 30°C
0.79 - 2.15
L-valine-4-nitroanilide
0.00229 - 3.31
Leu-4-nitroanilide
0.16 - 5
Lys-4-nitroanilide
0.58
Met-4-nitroanilide
pH 8.0, 30°C
0.18
Val-4-nitroanilide
pH 8.0, 30°C
additional information
additional information
-
2.4
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Cd2+-enzyme
3
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Ni2+-enzyme
4.9
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Mn2+-enzyme
7.9
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Co2+-enzyme
14.9
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Zn2+-enzyme
0.16
Arg-4-nitroanilide
-
-
0.16
Arg-4-nitroanilide
-
37°C, 0.5 mM CoCl2
3.8
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
3.9
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
4.5
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Zn2+-enzyme
4.5
bis(4-nitrophenyl) phosphate
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
9.5
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Co2+-enzyme
9.5
bis(4-nitrophenyl) phosphate
-
in presence of Co-Co-homo-dinuclear aminopeptidase
9.7
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Cd2+-enzyme
9.7
bis(4-nitrophenyl) phosphate
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
10.6
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Ni2+-enzyme
10.6
bis(4-nitrophenyl) phosphate
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
11
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
12
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Mn2+-enzyme
12.3
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
12.8
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
3.84
L-alanine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
4.81
L-alanine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
0.25
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221I
0.33
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant enzyme, in absence of Ca2+
0.34
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant enzyme, in presence of Ca2+
0.36
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme
0.58
L-Leu-4-nitroanilide
-
pH 8.0, 30°C
0.65
L-Leu-4-nitroanilide
-
pH 8.0, 37°C, recombinant enzyme, in presence of Ca2+
0.68
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221A
2.3
L-Leu-4-nitroanilide
-
pH 8.0, 37°C, recombinant enzyme, in absence of Ca2+
2.54
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant D3A/D262G, in absence of Ca2+
2.61
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme, in absence of Ca2+
3.47
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant E196A, in presence of Ca2+
3.79
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant E196A, in absence of Ca2+
3.91
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant chimeric mutant, in presence of Ca2+
4.02
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant chimeric mutant, in absence of Ca2+
4.02
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme, in presence of Ca2+
4.07
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant D3A/D262G, in presence of Ca2+
8.31
L-Leu-NH2
pH 8.0, 37°C, recombinant mutant F221I
15.6
L-Leu-NH2
pH 8.0, 37°C, recombinant wild-type enzyme
42.7
L-Leu-NH2
pH 8.0, 37°C, recombinant mutant F221A
15.8
L-Leu-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
16.1
L-Leu-O-methyl ester
pH 8.0, 37°C, recombinant mutant F221I
0.55
L-leucine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
0.67
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, native aminopeptidases 1 and 2
0.72
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, acetylated aminopeptidases 1 and 2
2.97
L-leucine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
0.34
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme
0.44
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221A
1.85
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221I
6.98
L-Phe-NH2
pH 8.0, 37°C, recombinant wild-type enzyme
7.68
L-Phe-NH2
pH 8.0, 37°C, recombinant mutant F221A
24.2
L-Phe-NH2
pH 8.0, 37°C, recombinant mutant F221I
6.9
L-Phe-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
12.8
L-Phe-O-methyl ester
pH 8.0, 37°C, recombinant mutant F221A
0.79
L-valine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
2.15
L-valine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
0.00229
Leu-4-nitroanilide
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
0.00242
Leu-4-nitroanilide
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
0.093
Leu-4-nitroanilide
-
in presence of Co-Co-homo-dinuclear aminopeptidase
0.15
Leu-4-nitroanilide
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
0.19
Leu-4-nitroanilide
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
0.213
Leu-4-nitroanilide
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
0.45
Leu-4-nitroanilide
pH 8.0, 30°C
0.88
Leu-4-nitroanilide
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
3.27
Leu-4-nitroanilide
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
3.31
Leu-4-nitroanilide
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
0.16
Lys-4-nitroanilide
-
-
0.16
Lys-4-nitroanilide
-
37°C, 0.5 mM CoCl2
5
Lys-4-nitroanilide
pH 8.0, 30°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
kinetics of recombinant wild-type and F221 mutant enzymes
-
additional information
additional information
kinetic analysis, effects of pH, solvent isotope effects, overview
-
additional information
additional information
-
kinetic analysis, effects of pH, solvent isotope effects, overview
-
additional information
additional information
-
kinetics,enzyme-substrate interaction, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0033 - 0.022
4-nitrophenyl phenylphosphonate
4.9
Ala-4-nitroanilide
pH 8.0, 30°C
0.0064 - 0.74
bis(4-nitrophenyl) phosphate
0.42
bis(p-nitrophenyl)phosphate
pH 8.0, 30°C
1.1
Gly-4-nitroanilide
pH 8.0, 30°C
1.71 - 2.94
L-Ala-4-nitroanilide
0.47 - 2.94
L-alanine-4-nitroanilide
0.49 - 391
L-Leu-4-nitroanilide
64.2 - 169
L-Leu-O-methyl ester
1.31 - 153
L-leucine-4-nitroanilide
17.6 - 229
L-Phe-4-nitroanilide
0.64 - 224
L-Phe-O-methyl ester
0.191
L-Val-4-nitroanilide
-
pH 8.0, 30°C
0.13 - 0.26
L-valine-4-nitroanilide
0.0433 - 657
Leu-4-nitroanilide
2.8
Lys-4-nitroanilide
pH 8.0, 30°C
43.3
Met-4-nitroanilide
pH 8.0, 30°C
0.28
Val-4-nitroanilide
pH 8.0, 30°C
0.0033
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Ni2+-enzyme
0.01
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Mn2+-enzyme
0.014
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Zn2+-enzyme
0.017
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Cd2+-enzyme
0.022
4-nitrophenyl phenylphosphonate
-
pH 8.0, 50°C, Co2+-enzyme
0.0064
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
0.01
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Ni2+-enzyme
0.01
bis(4-nitrophenyl) phosphate
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
0.016
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
0.043
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Cd2+-enzyme
0.043
bis(4-nitrophenyl) phosphate
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
0.081
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
0.087
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
0.1
bis(4-nitrophenyl) phosphate
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
0.21
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Mn2+-enzyme
0.45
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Zn2+-enzyme
0.45
bis(4-nitrophenyl) phosphate
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
0.74
bis(4-nitrophenyl) phosphate
-
pH 8.0, 30°C, Co2+-enzyme
0.74
bis(4-nitrophenyl) phosphate
-
in presence of Co-Co-homo-dinuclear aminopeptidase
1.71
L-Ala-4-nitroanilide
-
pH 8.0, 30°C
2.94
L-Ala-4-nitroanilide
-
pH 8.0, 30°C
0.47
L-alanine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
1.81
L-alanine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
2.94
L-alanine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
0.49
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant E196A, in presence of Ca2+
0.55
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant E196A, in absence of Ca2+
0.97
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme, in presence of Ca2+
1.08
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant D3A/D262G, in presence of Ca2+
2.12
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme, in absence of Ca2+
2.71
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant D3A/D262G, in absence of Ca2+
3 - 6
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant D3A/D262G, in absence of Ca2+
4.72
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant chimeric mutant, in presence of Ca2+
5.2
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant chimeric mutant, in absence of Ca2+
34
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221A
41.5
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant enzyme, in absence of Ca2+
42.1
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant enzyme, in presence of Ca2+
65.9
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme
75.3
L-Leu-4-nitroanilide
-
pH 8.0, 37°C, recombinant enzyme, in absence of Ca2+
108
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221I
223
L-Leu-4-nitroanilide
-
pH 8.0, 37°C, recombinant enzyme, in presence of Ca2+
391
L-Leu-4-nitroanilide
-
pH 8.0, 30°C
31.7
L-Leu-NH2
pH 8.0, 37°C, recombinant mutant F221A
104
L-Leu-NH2
pH 8.0, 37°C, recombinant wild-type enzyme
155
L-Leu-NH2
pH 8.0, 37°C, recombinant mutant F221I
64.2
L-Leu-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
142
L-Leu-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
169
L-Leu-O-methyl ester
pH 8.0, 37°C, recombinant mutant F221I
1.31
L-leucine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
75
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, acetylated aminopeptidases 2
111
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, native aminopeptidases 2
116
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, acetylated aminopeptidases 1
153
L-leucine-4-nitroanilide
-
pH 8.0, 22°C, native aminopeptidases 1
17.6
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant wild-type enzyme
19.3
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221I
229
L-Phe-4-nitroanilide
pH 8.0, 37°C, recombinant mutant F221A
10.7
L-Phe-NH2
pH 8.0, 37°C, recombinant mutant F221I
43.8
L-Phe-NH2
pH 8.0, 37°C, recombinant wild-type enzyme
115
L-Phe-NH2
pH 8.0, 37°C, recombinant mutant F221A
0.64
L-Phe-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
54.3
L-Phe-O-methyl ester
pH 8.0, 37°C, recombinant wild-type enzyme
224
L-Phe-O-methyl ester
pH 8.0, 37°C, recombinant mutant F221A
0.13
L-valine-4-nitroanilide
-
pH 8.0, 30°C, in absence of Ca2+
0.26
L-valine-4-nitroanilide
-
pH 8.0, 30°C, in presence of Ca2+
0.0433
Leu-4-nitroanilide
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
0.0505
Leu-4-nitroanilide
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
1.5
Leu-4-nitroanilide
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
1.68
Leu-4-nitroanilide
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
27.5
Leu-4-nitroanilide
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
37.4
Leu-4-nitroanilide
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
41
Leu-4-nitroanilide
-
in presence of Co-Co-homo-dinuclear aminopeptidase
92.8
Leu-4-nitroanilide
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
101
Leu-4-nitroanilide
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
657
Leu-4-nitroanilide
pH 8.0, 30°C
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0.000011 - 0.00079
amastatin
2.31
bis(p-nitrophenyl)phosphate
pH 5.0, 30°C
36.6
D-phenylalanine
-
pH 8.0, 30°C, in presence of Ca2+
0.0005 - 0.0055
L-leucine chloromethyl ketone
12.7
L-phenylalanine
-
pH 8.0, 30°C, in presence of Ca2+
0.0019 - 0.0053
L-phenylalanine chloromethyl ketone
10.3
leucine
pH 8.0, 30°C
additional information
additional information
-
0.000011
amastatin
-
pH 8.0, 37°C, recombinant enzyme
0.000016
amastatin
-
pH 8.0, 30°C, in presence of Ca2+
0.00055
amastatin
-
pH 8.0, 30°C, in absence of Ca2+
0.00079
amastatin
pH 8.0, 37°C, recombinant enzyme
0.0026
bestatin
-
pH 8.0, 30°C, in presence of Ca2+
0.0039
bestatin
-
pH 8.0, 37°C, recombinant enzyme
0.0054
bestatin
-
pH 8.0, 30°C, in absence of Ca2+
0.065
bestatin
pH 8.0, 37°C, recombinant enzyme
1.1
fluoride
-
substrate Leu-4-nitroanilide, in presence of Mn-Mn-homo-dinuclear aminopeptidase
17
fluoride
-
substrate Leu-4-nitroanilide, in presence of Mn-Co-hetero-dinuclear aminopeptidase
28
fluoride
-
substrate Leu-4-nitroanilide, in presence of Co-Co-homo-dinuclear aminopeptidase
70
fluoride
-
substrate Leu-4-nitroanilide, in presence of Mn-Zn-hetero-dinuclear aminopeptidase
75
fluoride
-
substrate Leu-4-nitroanilide, in presence of Mn-Ni-hetero-dinuclear aminopeptidase
82
fluoride
-
substrate Leu-4-nitroanilide, in presence of Ni-Ni-homo-dinuclear aminopeptidase
108
fluoride
-
substrate Leu-4-nitroanilide, in presence of Zn-Zn-homo-dinuclear aminopeptidase
12.4
L-leucine
-
pH 8.0, 30°C, in presence of Ca2+
12.8
L-leucine
-
pH 6.5, 30°C, in presence of Ca2+
29
L-leucine
-
above, pH 8.0, 37°C, recombinant enzyme
100
L-leucine
above, pH 8.0, 37°C, recombinant enzyme
0.0005
L-leucine chloromethyl ketone
-
pH 8.0, 30°C, in presence of Ca2+
0.0055
L-leucine chloromethyl ketone
-
pH 8.0, 30°C, in absence of Ca2+
8.7
L-methionine
-
pH 8.0, 30°C, in presence of Ca2+
9.1
L-methionine
-
pH 6.5, 30°C, in presence of Ca2+
0.0019
L-phenylalanine chloromethyl ketone
-
pH 8.0, 30°C, in presence of Ca2+
0.0053
L-phenylalanine chloromethyl ketone
-
pH 8.0, 30°C, in absence of Ca2+
additional information
additional information
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
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purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M HEPES/NaOH, pH 7.6, 2.0 M ammonium sulfate, and 2% PEG 400, 4 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
hanging drop vapour diffusion method, 18-25 mg/ml purified enzyme in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM CaCl2, plus an equal volume of sodium acetate buffer at pH 5.0 to 6.0, 16-20% w/v polyethylene glycol 4000, suspended over 1 ml reservoir solution of sodium acetate, pH 5.0-6.0, 16-20% PEG 4000, 3-4 weeks, X-ray diffraction structure determination at 47.2 to 1.9 A resolution and analysis
-
protein with or without bound Zn2+ or replaced with Hg2+, hanging drop vapour diffusion method, 20 mg/ml purified enzyme in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM CaCl2, plus an equal volume of sodium acetate buffer at pH 5.0 to 6.0, 16-20% w/v polyethylene glycol 4000, suspended over 1 ml reservoir solution of sodium acetate, pH 5.0-6.0, 16-20% PEG 4000, 4-5 weeks to full size crystals, X-ray diffraction structure determination at 2.1 to 1.75 A resolution and analysis
-
purified enzyme complexed with L-methionine, L-phenylalanine, or L-leucine, hanging-drop vapour diffusion method, protein solution: 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, 100 mM L-methionine or 200 mM L-leucine, plus equal volume of precipitant solution: 24% w/v PEG 4000, 0.1 M ammonium sulfate, equilibrated against 1 ml of reservoir precipitant solution, 3-4 days, cyrstals of enzyme complexed with L-Phe were precipitated with 0.1 M acetate buffer, pH 5.5 instead in the same procedure within 8-10 weeks, X-ray complex structure determination at 1.6 A resolution and analysis
-
purified enzyme complexed with methionine, hanging-drop vapour diffusion method, protein solution: 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, 0.1 M methionine, plus equal volume of precipitant solution: 24% w/v PEG 4000, 0.1 M ammonium sulfate, equilibrated against 1 ml reservoir of the precipitant solution, 3-4 days, X-ray diffraction structure determination at 1.53 A high resolution and analysis
purified enzyme in complex with tryptophan or 4-iodo-L-phenylalanine, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM tryptophan or 2 mM 4-iodo-L-phenylalanine, equal volumes of protein and reservoir solution are mixed, the latter containing 18% w/v PEG 4000 and 0.1 M sodium acetate, pH 5.5, equilibration against 1 ml reservoir solution for 1 day, microseeding, 3-4 days, X-ray diffraction structure determination and analysis at 1.3 A resolution
-
purified native enzyme in complex with product analogous weak inhibiting amino acids phenylalanine, leucine, and methionine, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM L-methionine or 200 mM L-leucine, the precipitant solution contains 24% w/v PEG 4000 and 0.1 M ammonium sulfate, equilibration against 1 ml reservoir solution, microseeding, 3-4 days, with phenylalanine a protein solution containing 18 mg/ml protein, 10 mM Tris-HCl, pH 8.0, 20 mM NaCl, 6 mM CaCl2, and 100 mM Phe is mixed with a reservoir solution containing 18% w/v PEG 4000, and 0.1 M acetate buffer, pH 5.5, microseeding, 3-4 days, X-ray diffraction structure determination and analysis at 1.8 A, 1.7 A, and 1.53 A resolution, respectively, structure modelling
structure determination and analysis
-
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Gilboa, R.; Greenblatt, H.M.; Perach, M.; Spungin-Bialik, A.; Lessel, U.; Wohlfahrt, G.; Schomburg, D.; Blumberg, S.; Shoham, G.
Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 A resolution
Acta Crystallogr. Sect. D
D56
551-558
2000
Streptomyces griseus, Streptomyces griseus (P80561)
brenda
Spungin, A.; Blumberg, S.
Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme
Eur. J. Biochem.
183
471-477
1989
Streptomyces griseus (P80561), Streptomyces griseus
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Ben-Meir, D.; Spungin, A.; Ashkenazi, R.; Blumberg, S.
Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution
Eur. J. Biochem.
212
107-112
1993
Streptomyces griseus
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Maras, B.; Greenblatt, H.M.; Shoham, G.; Spungin-Bialik, A.; Blumberg, S.; Barra, D.
Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases
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236
843-846
1996
Streptomyces griseus (P80561)
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Inhibition of Streptomyces griseus aminopeptidase and effects of calcium ions on catalysis and binding--comparisons with the homologous enzyme Aeromonas proteolytica aminopeptidase
Eur. J. Biochem.
258
313-319
1998
Streptomyces griseus
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Vosbeck, K.D.; Greenberg, B.D.; Awad, W.M., Jr.
The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Specificity and immobilization of aminopeptidase
J. Biol. Chem.
250
3981-3987
1975
Streptomyces griseus
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Almog, O.; Greenblatt, H.M.; Spungin, A.; Ben-Meir, D.; Blumberg, S.; Shoham, G.
Crystallization and preliminary crystallographic analysis of Streptomyces griseus aminopeptidase
J. Mol. Biol.
230
342-344
1993
Streptomyces griseus
brenda
Greenblatt, H.M.; Almog, O.; Maras, B.; Spungin-Bialik, A.; Barra, D.; Blumberg, S.; Shoham, G.
Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 A resolution
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265
620-636
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Streptomyces griseus
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Purification and characterization of recombinant Streptomyces griseus aminopeptidase
Protein Expr. Purif.
30
62-68
2003
Streptomyces griseus
brenda
Gilboa, R.; Spungin-Bialik, A.; Wohlfahrt, G.; Schomburg, D.; Blumberg, S.; Shoham, G.
Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism
Proteins
44
490-504
2001
Streptomyces griseus
brenda
Reiland, V.; Gilboa, R.; Spungin-Bialik, A.; Schomburg, D.; Shoham, Y.; Blumberg, S.; Shoham, G.
Binding of inhibitory aromatic amino acids to Streptomyces griseus aminopeptidase
Acta Crystallogr. Sect. D
60
1738-1746
2004
Streptomyces griseus
brenda
Jankiewicz, U.; Bielawski, W.
The properties and functions of bacterial aminopeptidases
Acta Microbiol. Pol.
52
217-231
2003
Streptomyces griseus
brenda
Arima, J.; Uesugi, Y.; Iwabuchi, M.; Hatanaka, T.
Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis
Appl. Environ. Microbiol.
71
7229-7235
2005
Streptomyces septatus (Q75V72), Streptomyces septatus TH-2 (Q75V72)
brenda
Arima, J.; Iwabuchi, M.; Hatanaka, T.
Gene cloning and overproduction of an aminopeptidase from Streptomyces septatus TH-2, and comparison with a calcium-activated enzyme from Streptomyces griseus
Biochem. Biophys. Res. Commun.
317
531-538
2004
Streptomyces griseus, Streptomyces septatus (Q75V72), Streptomyces septatus TH-2 (Q75V72), Streptomyces septatus TH-2
brenda
Ercan, A.; Park, H.I.; Ming, L.J.
Remarkable enhancement of the hydrolyses of phosphoesters by dinuclear centers: Streptomyces aminopeptidase as a 'natural model system'
Chem. Commun. (Camb.)
1
2501-2502
2000
Streptomyces sp.
-
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Fundoiano-Hershcovitz, Y.; Rabinovitch, L.; Langut, Y.; Reiland, V.; Shoham, G.; Shoham, Y.
Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus
FEBS Lett.
571
192-196
2004
Streptomyces griseus
brenda
Herrera-Camacho, I.; Lopez-Garcia, A.; Millan-Perez-Pena, L.
Aminopeptidase yscCO-II
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
1016-1017
2004
Saccharomyces cerevisiae
-
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Awad, W.M., Jr.
Streptomyces griseus aminopeptidase
Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rowlings, N. D. ; Woessner, J. F. , eds. )
1
957-959
2004
Streptomyces griseus, Streptomyces griseus K-1
-
brenda
Odintsov, S.G.; Sabala, I.; Bourenkov, G.; Rybin, V.; Bochtler, M.
Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan
J. Biol. Chem.
280
27792-27799
2005
Staphylococcus aureus, Staphylococcus aureus NCTC8325-4
brenda
Arima, J.; Uesugi, Y.; Uraji, M.; Yatsushiro, S.; Tsuboi, S.; Iwabuchi, M.; Hatanaka, T.
Modulation of Streptomyces leucine aminopeptidase by calcium: identification and functional analysis of key residues in activation and stabilization by calcium
J. Biol. Chem.
281
5885-5894
2006
Streptomyces griseus (Q5WA30), Streptomyces griseus
brenda
Hasselgren, C.; Park, H.I.; Ming, L.J.
Metal ion binding and activation of Streptomyces griseus dinuclear aminopeptidase: cadmium(II) binding as a model
J. Biol. Inorg. Chem.
6
120-127
2001
Streptomyces griseus
brenda
Herrera-Camacho, I.; Morales-Monterrosas, R.; Quiroz-Alvarez, R.
Aminopeptidase yscCo-II: a new cobalt-dependent aminopeptidase from yeast-purification and biochemical characterization
Yeast
16
219-229
2000
Saccharomyces cerevisiae
brenda
Ercan, A.; Park, H.I.; Ming, L.-J.
A moonlighting dizinc aminopeptidase from Streptomyces griseus: mechanisms for peptide hydrolysis and the 4 x 1010-fold acceleration of the alternative phosphodiester hydrolysis
Biochemistry
45
13779-13793
2006
Streptomyces griseus (P80561), Streptomyces griseus
brenda
Hershcovitz, Y.F.; Gilboa2, R.; Reiland, V.; Shoham, G.; Shoham, Y.
Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus
FEBS J.
274
3864-3876
2007
Streptomyces griseus
brenda
Arima, J.; Morimoto, M.; Usuki, H.; Mori, N.; Hatanaka, T.
The aminolysis reaction of streptomyces S9 aminopeptidase promotes the synthesis of diverse prolyl dipeptides
Appl. Environ. Microbiol.
76
4109-4112
2010
Streptomyces thermocyaneoviolaceus
brenda
Usuki, H.; Uesugi, Y.; Arima, J.; Yamamoto, Y.; Iwabuchi, M.; Hatanaka, T.
Engineered transaminopeptidase, aminolysin-S for catalysis of peptide bond formation to give linear and cyclic dipeptides by one-pot reaction
Chem. Commun. (Camb. )
46
580-582
2010
Streptomyces thermocyaneoviolaceus, Streptomyces thermocyaneoviolaceus NBRC14271
brenda
Arima, J.; Morimoto, M.; Usuki, H.; Mori, N.; Hatanaka, T.
Beta-alanyl peptide synthesis by Streptomyces S9 aminopeptidase
J. Biotechnol.
147
52-58
2010
Streptomyces thermocyaneoviolaceus, Streptomyces thermocyaneoviolaceus NBRC14271
brenda
Ercan, A.; Tay, W.M.; Grossman, S.H.; Ming, L.J.
Mechanistic role of each metal ion in Streptomyces dinuclear aminopeptidase: PEPTIDE hydrolysis and 7x10(10)-fold rate enhancement of phosphodiester hydrolysis
J. Inorg. Biochem.
104
19-29
2010
Streptomyces griseus
brenda