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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
active site structure involving His97, Asp117, Asp179, Glu151, Glu152, and His256
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure and mechanism
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism involving divalent metal ions, overview
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism involving the two zinc ions
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
presence of at least one active Tyr and one carboxyl group demonstrated by chemical modifications of enzyme: nitration, azotization, diethyldirocarbonate treatment, 1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treatment
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
mechanism. Substrate only binds to the first metal binding site
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
catalytic mechanism
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
substrate binding mechanism and structure
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis
-
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
structure-activity relationship, active site structure involving zinc-binding ligands His97, Asp117, Asp179, Glu151, Glu152, and His256
-
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L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucyl-L-leucyl-L-leucine + H2O
L-leucine + L-leucyl-L-leucine
-
-
-
?
recombinant human methionine-interferon alpha-2b + H2O
L-methionine + recombinant human interferon alpha-2b
-
-
-
?
Ala-Gly + H2O
Ala + Gly
-
-
-
ir
DL-Ala-Gly-Gly + H2O
DL-Ala + Gly-Gly
-
-
-
ir
DL-Leu-Gly-DL-Phe + H2O
DL-Leu + Gly-DL-Phe
-
-
-
ir
DL-Leu-Gly-Gly + H2O
DL-Leu + Gly-Gly
-
-
-
ir
Ile-amide + H2O
Ile + NH3
-
-
-
ir
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine anilide + H2O
L-leucine + aniline
-
-
-
?
L-leucine ethyl ester + H2O
L-leucine + ethanol
-
-
-
?
L-leucine-4-anisidide + H2O
L-leucine + anisidine
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-amide + H2O
Leu + NH3
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
Leu-Gly + H2O
Leu + Gly
-
-
-
ir
Leu-methyl ester + H2O
Leu + methanol
-
-
-
ir
Lys-Gly + H2O
Lys + Gly
-
-
-
ir
Met-amide + H2O
Met + NH3
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
norvalinamide + H2O
norvaline + NH3
-
-
-
-
?
Peptides + H2O
?
-
-
81170, 81171, 81172, 81173, 81174, 81175, 81176, 81177, 81178, 81179, 81180, 81181, 81182, 81183, 81184, 81185, 81186, 81187, 81189, 81190 -
-
?
peptides + H2O
N-terminal amino acid + peptide(n-1)
-
-
-
?
Phe-amide + H2O
Phe + NH3
-
-
-
ir
Phe-Asp-Ser-Ala-Val + H2O
Phe + Asp-Ser-Ala-Val
-
-
-
ir
Phe-beta-naphthylamide + H2O
Phe + beta-naphthylamine
-
18% of rate of hydrolysis of Leu-beta-naphthylamide
-
ir
Phe-Gly + H2O
Phe + Gly
-
-
-
ir
Phe-methyl ester + H2O
Phe + methanol
-
-
-
ir
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
-
-
-
ir
Pro-Phe-Pro + H2O
Pro + Phe-Pro
-
-
-
ir
thionoleucine-4-anisidide + H2O
thionoleucine + anisidine
-
-
-
?
thionoleucine-S-anilide + H2O
thionoleucine + aniline
-
-
-
?
Thr-beta-naphthylamide + H2O
Thr + beta-naphthylamine
-
3.3% of rate of hydrolysis of Leu-beta-naphthylamide
-
ir
Tyr-Gly + H2O
Tyr + Gly
-
-
-
ir
Val-amide + H2O
Val + NH3
-
-
-
ir
Val-Gly + H2O
Val + Gly
-
-
-
ir
additional information
?
-
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
-
enzyme in solution and immobilized on synthetic Mg2+ and Al2+ ion-containing layered double hydroxide particles
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
ir
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
ir
Leu-Ala + H2O
Leu + Ala
-
-
-
ir
Leu-Ala + H2O
Leu + Ala
-
-
-
ir
Leu-amide + H2O
Leu + NH3
-
-
-
ir
Leu-amide + H2O
Leu + NH3
-
-
-
ir
Leu-Arg + H2O
Leu + Arg
-
-
-
ir
Leu-Arg + H2O
Leu + Arg
-
-
-
ir
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
ir
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
ir
Leu-Ile + H2O
Leu + Ile
-
-
-
ir
Leu-Ile + H2O
Leu + Ile
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
-
-
-
ir
Leu-Met + H2O
Leu + Met
-
-
-
ir
Leu-Met + H2O
Leu + Met
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
-
-
-
ir
Leu-Trp + H2O
Leu + Trp
-
-
-
ir
Leu-Trp + H2O
Leu + Trp
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Tyr + H2O
Leu + Tyr
-
-
-
ir
Leu-Val + H2O
Leu + Val
-
-
-
ir
Leu-Val + H2O
Leu + Val
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
-
-
-
ir
additional information
?
-
the enzyme shows broad substrate specificity
-
-
?
additional information
?
-
investigation of the mode of action using a quantum mechanical/molecular mechanical approach
-
-
?
additional information
?
-
recombinant enzyme rLAP is selective and specific to remove N-terminal groups from amino acids
-
-
?
additional information
?
-
-
difference in action towards oligopeptides and polypeptides, as compared to amides, may be due to ability of enzyme to bind larger substrates more effectively
-
-
?
additional information
?
-
-
also cleaved: gastrin peptide (carboxyterminal), various oligopeptides, Met-Lys-bradykinin, adrenocorticotropic hormone, glucagon, aminoethylated B-chain insulin, sperm whale myoglobin, ribunuclease, beta-lactoglobulin, egg white lysozyme, aminoethylated lysozyme
-
-
?
additional information
?
-
-
also cleaved: gastrin peptide (carboxyterminal), various oligopeptides, Met-Lys-bradykinin, adrenocorticotropic hormone, glucagon, aminoethylated B-chain insulin, sperm whale myoglobin, ribunuclease, beta-lactoglobulin, egg white lysozyme, aminoethylated lysozyme
-
-
?
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
-
-
?
additional information
?
-
-
the enzyme prefers substrates with large and hydrophobic N-terminal amino acid 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
-
-
?
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Co2+
2 Co2+ bound at the dinuclear active site, can be substituted by Zn2+, binding mode
Co2+
can substitute for Zn2+
Zn2+
2 Zn2+ bound at the dinuclear active site, can be substituted by Co2+, binding mode
Zn2+
bound in the active site, binding structure, bridged bimetallic enzyme
Zn2+
AAP is a metalloenzyme containing two Zn2+ per enzyme molecule
Zn2+
dinuclear Zn2+ metal center, the binding of Zn2+ to the E151H mutant is much more weak than to the wild-type enzyme
Zn2+
the enzyme is bridged bimetallic, the metal ions are involved in the reaction, overview
Zn2+
the metallopeptidase requires two divalent metal ions per enzyme molecule for full activity, binuclear metal center activation and reaction mechanism
Zn2+
AAP is a binuclear zinc enzyme, Zn2+ is essential for its enzymatic activity
Zn2+
two zinc ions in close proximity have been identified to form the metal component of the active site
Zn2+
required, 2 Zn2+ per active site
Cd2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Cd2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
-
Co2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Co2+
-
65% of activity of zinc enzyme
Co2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Co2+
-
spectroscopically distinct cobalt sites in heterodimetallic enzymes, implications for substrate binding
Co2+
-
Co2+ can substitute for Cd2+ in the bimetallic enzyme
Co2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
can substitute for one or both Zn2+ ions
Co2+
-
Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Co2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Cu2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Cu2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Mn2+
-
-
Mn2+
-
58% of activity of zinc enzyme
Ni2+
-
-
Ni2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Zn2+
-
-
Zn2+
-
bound zinc ion interacts directly with substrate during catalysis but not during substrate binding, contains 2 mol zinc per mol enzyme but only one site has to be occupied in order to faciliate catalysis
Zn2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than in the opposite sequence, which suggests two metal-binding sites with different functions
Zn2+
-
2 mol zinc per mol enzyme
Zn2+
-
no loss of zinc upon photoinactivation
Zn2+
-
zinc can be replaced by other metals, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of metal ions, sequence of addition effects activity
Zn2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Zn2+
-
dinuclear Zn2+ metal center
Zn2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Zn2+
-
the enzyme is a two-zinc metallopeptidase, zinc-binding involved residues His97, Asp117, Glu152, Asp179, and His256
Zn2+
-
zinc-dependent metallopeptidase, Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Zn2+
-
zinc-metallopeptidase, 2 ions per enzyme molecule
additional information
detailed metal binding structure analysis, overview, the first metal ion in the dinuclear metal center is in a hexacoordinate/pentacoordinate equilibrium, while the second metal ion is six-coordinate
additional information
-
metal ion interacts directly with the substrate atoms, as shown by multiple inhibitor studies
additional information
-
bimetallic enzyme, binding conformations, overview
additional information
-
detailed metal binding structure and kinetic analysis with recombinant wild-type and mutant enzymes, overview
additional information
-
metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
-
metalloprotein active site, structure and mechanism overview
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1-butaneboronic acid
binding mode
4-iodo-D-phenylalanine hydroxamate
binding mode
DTT
complete inhibition at 20 mM
L-leucine
competitive inhibition
L-leucine 4-nitroanilide
-
L-leucine phosphonic acid
binding mode
L-leucinephosphonic acid
competitive, interacts with both metal ions in the dinuclear active site, inhibition mechanism
leucine phosphonic acid
competitive inhibition
n-valeramide
enzyme-inhibitor complex represents snapshot of proteolytic reaction between Michaelis-Menten and transition state
1,2-Cyclohexanedione
-
Ki: 0.022-0.023 mM
1-butaneboronic acid
-
binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
2,3-Butanedione
-
photochemical inactivation: effect only in the light, proportional to light intensity, modification of 5 Trp-, 3-4 Tyr-, 2 His- and 2Arg-residues, no photoinactivation in the absence of oxygen or in the presence of azide, protection also by Trp, Met, D-Met, L-2-thiol-His, 2-mercaptoethanol, Gly-Met, Ki: 5.1-19.8 mM
2,3-Pentanedione
-
photochemical inactivation: effect only in UV-light
2-amino-1,4-dihydro-2-isoquinolin-3-one
-
-
2-aminocycloheptanone
-
-
2-hydroxy-1,4-dihydro-2H-isoquinolin-3-one
-
-
2-methylquinolin-8-ol
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-carbohydroxamic acid
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-ethanone
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-phosphonic acid
-
-
3-amino-3,4-dihydro-1H-naphtalen-2-one
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(2-phenylethyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(3-phenylpropyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(4-phenylbutyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(5-phenylpentyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-benzyloxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-methyloxime
-
-
3-methyl-1,2-cyclopentanedione
-
Ki: 0.48-1.19 mM
3-methyl-1-butanol
-
Ki: 0.98 mM
3-methylquinolin-8-ol
-
-
4-iodo-D-phenylalanine hydroxamate
-
-
5,7-dibromoquinolin-8-ol
-
-
5,7-dichloroquinolin-8-ol
-
-
5,7-diiodoquinolin-8-ol
-
-
5-(trifluoromethyl)quinolin-8-ol
-
-
5-bromo-2-methylquinolin-8-ol
-
-
5-bromo-8-hydroxy-2-methylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,2-dimethylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,N,2-trimethylquinoline-7-sulfonamide
-
-
5-chloro-2-methylquinolin-8-ol
-
-
5-chloro-7-iodoquinolin-8-ol
-
-
5-chloro-8-hydroxy-N,N-dimethylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxy-N-methylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxyquinoline-7-sulfonamide
-
-
5-chloroquinolin-8-ol
-
-
5-fluoroquinolin-8-ol
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-oxime
-
-
8-hydroxy-N,N-dimethylquinoline-5-sulfonamide
-
-
amastatin
-
reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1
Amino acid hydroxamates
-
-
benzyl alcohol
-
Ki: 2.6 mM
cysteine
-
60% loss of activity at 10 mM
D-Leu-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Leu-hydroxamate
-
Ki: 2 nM, L-isomer bound 150 times less tightly
D-Val-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Val-hydroxamate
-
Ki: 5 nM
DL-Ala-hydroxamate
-
Ki: 0.0055 mM
DL-Phe-hydroxamate
-
Ki: 0.0008 mM
DL-Thr-hydroxamate
-
Ki: 0.002 mM
DL-Val-hydroxamate
-
Ki: 10 nM
epibestatin
-
Ki: 0.07 mM
L-Ala-hydroxamate
-
Ki: 0.02 mM
L-leucine phosphonic acid
-
transition state inhibitor, binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
L-Phe-hydroxamate
-
Ki: 0.0088 mM
L-Thr-hydroxamate
-
Ki: 0.066 mM
L-Val-hydroxamate
-
Ki: 0.0022 mM
methylglyoxal
-
photochemical inactivation: effect only in UV-light, Ki: 1.8-2.0 mM
N-mercapto-leucyl-4-nitroanilides
-
-
N-mercaptoacyl-leucyl-p-nitroaniline
-
synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition, Ki: 2.5-57 nM
-
n-valeramide
-
no effect on enzyme zinc uptake, Ki: 0.0006 mM
Na2S
-
60% loss of activity at 10 mM
p-iodo-D-Phe hydroxamate
-
structure of enzyme-inhibitor complex: Glu151 has crucial functional role
t-butyloxycarbonyl-L-Leu
-
bromomethyl ketone derivative, utilized for purification procedure
Thioglycollate
-
60% loss of activity at 10 mM
thionoleucine-S-anilide
-
-
thionoleucine-S-anisidide
-
-
Tris
chelated to active site Zn2+
1-Butaneboronate
-
-
1-Butaneboronate
-
enhances zinc uptake by enzyme, Ki: 0.0027 mM
1-Phenyl-2-thiourea
-
-
1-Phenyl-2-thiourea
-
competitive
bestatin
-
-
bestatin
-
reversible, slow, tight binding, transition state analog complex, Ki: 18 nM, stoichiometry of inhibition 1:1
EDTA
-
-
EDTA
-
complete inactivation, reversible by Zn2+, Co2+, Ni2+, or Cu2+
L-leucinethiol
-
-
L-leucinethiol
-
i.e. LeuSH, kinetic and spectroscopic characterization of the slow, tight-binding peptide inhibitor-enzyme complex, inhibition mechanism
Leu-bromomethyl ketone
-
reversible, Ki: 200 nM
Leu-bromomethyl ketone
-
succinamic acid derivative, Ki: 0.0069 mM
Leu-chloromethyl ketone
-
succinimido derivative, reversible, Ki: 0.17 mM
Leu-chloromethyl ketone
-
reversible, Ki: 670 nM
Leu-methyl ketone
-
reversible, Ki: 0.018 mM
Leu-methyl ketone
-
derivatives
Leu-methyl ketone
-
derivatives, Ki: 0.14 - 0.17 mM
Phenylglyoxal
-
-
Phenylglyoxal
-
Ki: 0.002-0.0023 mM
additional information
the propeptides internally inhibits the enzyme in the 54 kDa zymogen in a cooperative inhibitory interaction
-
additional information
-
-
-
additional information
-
multiple inhibition study with substrate analogs and transition state analogs
-
additional information
-
inhibited to a greater extend by D- than by L-hydroxamates of amino acids and aliphatic acids, pH-dependent
-
additional information
-
inhibition mechanisms, overview
-
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0.01 - 0.902
L-Leu-4-nitroanilide
0.01
L-leucine 4-nitroanilide
pH 8.0, 25°C
0.02726
recombinant human methionine-interferon alpha-2b
pH 6.0, 37°C
-
0.019 - 15
L-leucine 4-nitroanilide
45 - 78
L-leucine anilide
0.7
L-leucine ethyl ester
-
-
32 - 50
L-leucine-4-anisidide
0.43
Leu-beta-naphthylamide
-
-
4 - 7
thionoleucine-4-anisidide
4 - 11
thionoleucine-S-anilide
additional information
additional information
-
0.01
L-Leu-4-nitroanilide
mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.0106
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
0.013
L-Leu-4-nitroanilide
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.025
L-Leu-4-nitroanilide
mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.0317
L-Leu-4-nitroanilide
apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.245
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
0.311
L-Leu-4-nitroanilide
pH 8.0, 70°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
0.34
L-Leu-4-nitroanilide
mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.902
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation
0.019
L-leucine 4-nitroanilide
-
-
0.019 - 0.0215
L-leucine 4-nitroanilide
-
native enzyme, buffer dependent
0.02
L-leucine 4-nitroanilide
-
-
0.021
L-leucine 4-nitroanilide
-
native enzyme
0.028
L-leucine 4-nitroanilide
-
-
0.032
L-leucine 4-nitroanilide
-
diethylpyrocarbonate-treated enzyme
0.055
L-leucine 4-nitroanilide
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
0.06
L-leucine 4-nitroanilide
-
nitro-enzyme
0.126
L-leucine 4-nitroanilide
-
photoinactivated enzyme
0.136
L-leucine 4-nitroanilide
-
azo-enzyme
4.6
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
7.8
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
15
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
45
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
61
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
78
L-leucine anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
32
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
34
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
50
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
4
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
4
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
5
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
7
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
4
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
8
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
10
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
11
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
additional information
additional information
kinetics with metal-bound enzyme variants
-
additional information
additional information
kinetics of different native and recombinant enzyme forms, overview
-
additional information
additional information
pH-dependence of kinetics, isothermal titration measurement, thermodynamics, overview
-
additional information
additional information
thermodynamics and Michaelis-Menten kinetics, overview
-
additional information
additional information
-
amides and dipeptides
-
additional information
additional information
-
amides and dipeptides
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics of apoenzyme and metal-bound wild-type and mutant enzymes, isothermal titration measurement, thermodynamics, overview
-
additional information
additional information
-
kinetics with Zn and/or Cd-containing enzyme, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.017 - 73
L-Leu-4-nitroanilide
4320
L-leucine 4-nitroanilide
pH 8.0, 25°C
0.000853
recombinant human methionine-interferon alpha-2b
pH 6.0, 37°C
-
1.1 - 69
L-leucine 4-nitroanilide
6.3 - 16
L-leucine anilide
96
L-leucine ethyl ester
-
-
3.8 - 9.5
L-leucine-4-anisidide
29.6
Leu-beta-naphthylamide
-
-
7.5 - 12.2
thionoleucine-4-anisidide
7.7 - 23.3
thionoleucine-S-anilide
additional information
additional information
-
penultimative substituents influence rate of hydrolysis
-
0.017
L-Leu-4-nitroanilide
apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.033
L-Leu-4-nitroanilide
pH 8.0, recombinant mutant E151H
0.7
L-Leu-4-nitroanilide
mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.817
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation
1.6
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
7
L-Leu-4-nitroanilide
mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
15.8
L-Leu-4-nitroanilide
pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
48.45
L-Leu-4-nitroanilide
pH 8.0, 70°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)
60
L-Leu-4-nitroanilide
mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
65
L-Leu-4-nitroanilide
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
71.33
L-Leu-4-nitroanilide
pH 8.0, 25°C, mature wild-type enzyme
73
L-Leu-4-nitroanilide
pH 8.0, recombinant wild-type enzyme
1.1
L-leucine 4-nitroanilide
-
-
1.1
L-leucine 4-nitroanilide
-
photoinactivated enzyme
3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
4
L-leucine 4-nitroanilide
-
azo-enzyme
5.3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
14.3
L-leucine 4-nitroanilide
-
nitro-enzyme
42
L-leucine 4-nitroanilide
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
50 - 69
L-leucine 4-nitroanilide
-
native enzyme, buffer dependent
55.5
L-leucine 4-nitroanilide
-
diethylpyrocarbonate-treated enzyme
60
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
64
L-leucine 4-nitroanilide
-
-
67
L-leucine 4-nitroanilide
-
-
67.3
L-leucine 4-nitroanilide
-
native enzyme
6.3
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
15.1
L-leucine anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
16
L-leucine anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
3.8
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
9.3
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
9.5
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
7.5
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
7.9
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.1
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
12.2
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
7.7
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
10.6
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.5
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
16.9
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
23.3
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
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Baker, J.O.; Prescott, J.M.
A transition-state-analog inhibitor influences zinc-binding by Aeromonas aminopeptidase
Biochem. Biophys. Res. Commun.
130
1154-1160
1985
Vibrio proteolyticus
brenda
Wilkes, S.H.; Prescott, J.M.
The slow, tight binding of bestatin and amastatin to aminopeptidases
J. Biol. Chem.
260
13154-13162
1985
Vibrio proteolyticus
brenda
Prescott, J.M.; Wagner, F.W.; Holmquist, B.; Vallee, B.L.
Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites
Biochemistry
24
5350-5356
1985
Vibrio proteolyticus
brenda
Wilkes, S.H.; Prescott, J.M.
Stereospecificity of amino acid hydroxamate inhibition of aminopeptidases
J. Biol. Chem.
258
13517-13521
1983
Vibrio proteolyticus
brenda
Prescott, J.M.; Wagner, F.W.; Holmquist, B.; Vallee, B.L.
One hundred fold increased activity of Aeromonas aminopeptidase by sequential substitutions with Ni(II) or Cu(II) followed by zinc
Biochem. Biophys. Res. Commun.
114
646-652
1983
Vibrio proteolyticus
brenda
Baker, J.O.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.
Hydroxamates and aliphatic boronic acids: marker inhibitors for aminopeptidase
Biochemistry
22
2098-2103
1983
Vibrio proteolyticus
brenda
Prescott, J.M.; Wilkes, S.H.
Aeromonas aminopeptidase
Methods Enzymol.
45
530-543
1976
Vibrio proteolyticus
brenda
Kettner, C.; Glover, G.I.; Prescott, J.M.
Kinetics of inhibition of Aeromonas aminopeptidase by leucine methyl ketone derivatives
Arch. Biochem. Biophys.
165
739-743
1974
Vibrio proteolyticus
brenda
Kettner, C.; Rodriguez-Absi, J.; Glover, G.I.; Prescott, J.M.
The purification of Aeromonas aminopeptidase by affinity chromatography
Arch. Biochem. Biophys.
162
56-63
1974
Vibrio proteolyticus
brenda
Wagner, F.W.; Wilkes, S.H.; Prescott, J.M.
Specificity of Aeromonas aminopeptidase toward amino acid amides and dipeptides
J. Biol. Chem.
247
1208-1210
1972
Vibrio proteolyticus
brenda
Prescott, J.M.; Wilkes, S.H.; Wagner, F.W.; Wilson, K.J.
Aeromonas aminopeptidase. Improved isolation and some physical properties
J. Biol. Chem.
246
1756-1764
1971
Vibrio proteolyticus
brenda
Prescott, J.M.; Wilkes, S.H.
Aeromonas aminopeptidase: purification and some general properties
Arch. Biochem. Biophys.
117
328-336
1966
Vibrio proteolyticus
brenda
Maekinen, K.K.; Maekinen, P.L.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.
Chemical modification of Aeromonas aminopeptidase. Evidence for the involvement of tyrosyl and carboxyl groups in the activity of the enzyme
Eur. J. Biochem.
128
257-265
1982
Vibrio proteolyticus
brenda
Maekinen, K.K.; Maekinen, P.L.; Wilkes, S.H.; Bayliss, M.E.; Prescott, J.M.
Photochemical inactivation of Aeromonas aminopeptidase by 2,3-butanedione
J. Biol. Chem.
257
1765-1772
1982
Vibrio proteolyticus
brenda
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Specificity of aeromonas aminopeptidase toward oligopeptides and polypeptides
Eur. J. Biochem.
34
459-466
1973
Vibrio proteolyticus
brenda
Schalk, C.; Remy, J.M.; Chevrier, B.; Moras, D.; Tarnus, C.
Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data
Arch. Biochem. Biophys.
294
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1992
Vibrio proteolyticus
brenda
Bennett, B.; Holz, R.C.
Spectroscopically distinct cobalt(II) sites in heterodimetallic forms of the aminopeptidase from Aeromonas proteolytica: characterization of substrate binding
Biochemistry
36
9837-9846
1997
Vibrio proteolyticus
brenda
Chevrier, B.; D'Orchymont, H.; Schalk, C.; Moras, D.
The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit
Eur. J. Biochem.
237
393-398
1996
Vibrio proteolyticus
brenda
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1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development
Biochemistry
38
9048-9053
1999
Vibrio proteolyticus (Q01693)
brenda
Ustynyuk, L.; Bennett, B.; Edwards, T.; Holz, R.C.
Inhibition of the aminopeptidase from Aeromonas proteolytica by aliphatic alcohols. Characterization of the hydrophobic substrate recognition site
Biochemistry
38
11433-11439
1999
Vibrio proteolyticus
brenda
Huntington, K.M.; Bienvenue, D.L.; Wei, Y.; Bennett, B.; Holz, R.C.; Pei, D.
Slow-binding inhibition of the aminopeptidase from Aeromonas proteolytica by peptide thiols: synthesis and spectroscopic characterization
Biochemistry
38
15587-15596
1999
Vibrio proteolyticus
brenda
Stamper, C.; Bennett, B.; Edwards, T.; Holz, R.C.; Ringe, D.; Petsko, G.
Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis
Biochemistry
40
7035-7046
2001
Vibrio proteolyticus (Q01693)
brenda
Bienvenue, D.L.; Gilner, D.; Holz, R.C.
Hydrolysis of thionopeptides by the aminopeptidase from Aeromonas proteolytica: insight into substrate binding
Biochemistry
41
3712-3719
2002
Vibrio proteolyticus
brenda
Bienvenue, D.L.; Mathew, R.S.; Ringe, D.; Holz, R.C.
The aminopeptidase from Aeromonas proteolytica can function as an esterase
J. Biol. Inorg. Chem.
7
129-135
2002
Vibrio proteolyticus
brenda
Desmarais, W.T.; Bienvenue, D.L.; Bzymek, K.P.; Holz, R.C.; Petsko, G.A.; Ringe, D.
The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition
Structure
10
1063-1072
2002
Vibrio proteolyticus (Q01693)
brenda
Jankiewicz, U.; Bielawski, W.
The properties and functions of bacterial aminopeptidases
Acta Microbiol. Pol.
52
217-231
2003
Brevibacterium linens, Brevibacterium linens SR3, Escherichia coli, Lactococcus sp., Mycoplasma salivarium, Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Vibrio proteolyticus
brenda
Schuerer, G.; Lanig, H.; Clark, T.
Aeromonas proteolytica aminopeptidase: an investigation of the mode of action using a quantum mechanical/molecular mechanical approach
Biochemistry
43
5414-5427
2004
Vibrio proteolyticus (Q01693)
brenda
Bzymek, K.P.; Moulin, A.; Swierczek, S.I.; Ringe, D.; Petsko, G.A.; Bennett, B.; Holz, R.C.
Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica
Biochemistry
44
12030-12040
2005
Vibrio proteolyticus (Q01693)
brenda
Bennett, B.
EPR of Co(II) as a structural and mechanistic probe of metalloprotein active sites: characterisation of an aminopeptidase
Curr. Top. Biophys.
26
49-57
2002
Vibrio proteolyticus
-
brenda
Chevrier, B.; D'Orchymont, H.
Vibrio aminopeptidase
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
963-965
2004
Vibrio proteolyticus
-
brenda
Bzymek, K.P.; Swierczek, S.I.; Bennett, B.; Holz, R.C.
Spectroscopic and thermodynamic characterization of the E151D and E151A altered leucine aminopeptidases from Aeromonas proteolytica
Inorg. Chem.
44
8574-8580
2005
Vibrio proteolyticus
brenda
Bienvenue, D.L.; Bennett, B.; Holz, R.C.
Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinethiol: kinetic and spectroscopic characterization of a slow, tight-binding inhibitor-enzyme complex
J. Inorg. Biochem.
78
43-54
2000
Vibrio proteolyticus
brenda
Bzymek, K.P.; D'Souza, V.M.; Chen, G.; Campbell, H.; Mitchell, A.; Holz, R.C.
Function of the signal peptide and N- and C-terminal propeptides in the leucine aminopeptidase from Aeromonas proteolytica
Protein Expr. Purif.
37
294-305
2004
Vibrio proteolyticus (Q01693)
brenda
Kumar, A.; Periyannan, G.R.; Narayanan, B.; Kittell, A.W.; Kim, J.J.; Bennett, B.
Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus
Biochem. J.
403
527-536
2007
Vibrio proteolyticus (Q01693)
brenda
Albrecht, S.; Defoin, A.; Salomon, E.; Tarnus, C.; Wetterholm, A.; Haeggstroem, J.Z.
Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors
Bioorg. Med. Chem.
14
7241-7257
2006
Vibrio proteolyticus
brenda
Chen, S.; Marino, T.; Fang, W.; Russo, N.; Himo, F.
Peptide hydrolysis by the binuclear zinc enzyme aminopeptidase from Aeromonas proteolytica: A density functional theory study
J. Phys. Chem. B
112
2494-2500
2008
Vibrio proteolyticus (Q01693)
brenda
Ataie, N.J.; Hoang, Q.Q.; Zahniser, M.P.; Tu, Y.; Milne, A.; Petsko, G.A.; Ringe, D.
Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus
Biochemistry
47
7673-7683
2008
Vibrio proteolyticus (Q01693)
brenda
Hartley, M.; Bennett, B.
Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol
Protein Expr. Purif.
66
91-101
2009
Vibrio proteolyticus (Q01693)
brenda
Frey, S.T.; Guilmet, S.L.; Egan, R.G.; Bennett, A.; Soltau, S.R.; Holz, R.C.
Immobilization of the aminopeptidase from Aeromonas proteolytica on Mg2+/Al3+ layered double hydroxide particles
ACS Appl. Mater. Interfaces
2
2828-2832
2010
Vibrio proteolyticus
brenda
Albrecht, S.; Al-Lakkis-Wehbe, M.; Orsini, A.; Defoin, A.; Pale, P.; Salomon, E.; Tarnus, C.; Weibel, J.
Amino-benzosuberone: A novel warhead for selective inhibition of human aminopeptidase-N/CD13
Bioorg. Med. Chem.
19
1434-1449
2011
Vibrio proteolyticus
brenda
Perez-Sanchez, G.; Leal-Guadarrama, L.; Trelles, I.; Perez, N.; Medina-Rivero, E.
High-level production of a recombinant Vibrio proteolyticus leucine aminopeptidase and its use for N-terminal methionine excision from interferon alpha-2b
Process Biochem.
46
1825-1830
2011
Vibrio proteolyticus (Q01693)
-
brenda
Hanaya, K.; Suetsugu, M.; Saijo, S.; Yamato, I.; Aoki, S.
Potent inhibition of dinuclear zinc(II) peptidase, an aminopeptidase from Aeromonas proteolytica, by 8-quinolinol derivatives: inhibitor design based on Zn2+ fluorophores, kinetic, and X-ray crystallographic study
J. Biol. Inorg. Chem.
17
517-529
2012
Vibrio proteolyticus
brenda
Hernandez-Moreno, A.V.; Villasenor, F.; Medina-Rivero, E.; Perez, N.O.; Flores-Ortiz, L.F.; Saab-Rincon, G.; Luna-Barcenas, G.
Kinetics and conformational stability studies of recombinant leucine aminopeptidase
Int. J. Biol. Macromol.
64
306-312
2014
Vibrio proteolyticus (Q01693)
brenda