3.4.11.10: bacterial leucyl aminopeptidase
This is an abbreviated version!
For detailed information about bacterial leucyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.10
Reaction
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids =
Synonyms
AAP, Aeromonas proteolytica aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A (bacteria), aminopeptidase Ap1, aminopeptidase II, AP-II, API, APII, AVP, bacterial leucine aminopeptidase, bacterial M17 aminopeptidase, BSAP, Bsu aminopeptidase, BsuAP, CGase, cysteinylglycinase, double-zinc aminopeptidase, extracellular aminopeptidase, FgLAP, HpM17AP, LAP, LAPII, leucine aminopeptidase, leucine aminopeptidase II, leucine APN, Leucyl aminopeptidase, M17 aminopeptidase, M17 metallo-aminopeptidase, More, MtLAP, PepA, Peptidase A, pepZ, PhpA, ribosomal-bound aminopeptidase, rLAP55, Rv2213, SSAP, TAP, TH-2, thermophilic aminopeptidase, thermostable leucine aminopeptidase, Vibrio aminopeptidase, VpAP, ywaD
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3.4.11.10 bacterial leucyl aminopeptidaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.4.11.10 - bacterial leucyl aminopeptidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2,3-Butanedione
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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
amastatin
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reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1
Aprotinin
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the recombinant enzyme shows 58.9% relative activity in the presence of 0.001 mM aprotinin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
E-64
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the recombinant enzyme shows 43% relative activity in the presence of 0.005 mM E-64 on hydrolysis of L-Leu-7-amido-4-methylcoumarin
L-leucinephosphonic acid
competitive, interacts with both metal ions in the dinuclear active site, inhibition mechanism
Leu-chloromethyl ketone
-
reversible, Ki: 670 nM; succinimido derivative, reversible, Ki: 0.17 mM
leupeptin
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the recombinant enzyme shows 32.7% relative activity in the presence of 0.01 mM leupeptin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
methylglyoxal
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photochemical inactivation: effect only in UV-light, Ki: 1.8-2.0 mM
N-alpha-tosyl-L-lysine chlormethyl ketone
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the recombinant enzyme shows 28.9% relative activity in the presence of 0.005 mM N-alpha-tosyl-L-lysine chlormethyl ketone on hydrolysis of L-Leu-7-amido-4-methylcoumarin
N-mercaptoacyl-leucyl-p-nitroaniline
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synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition, Ki: 2.5-57 nM
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p-iodo-D-Phe hydroxamate
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structure of enzyme-inhibitor complex: Glu151 has crucial functional role
pepstatin A
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the recombinant enzyme shows 26.1% relative activity in the presence of 1 mM pepstatin A on hydrolysis of L-Leu-7-amido-4-methylcoumarin
t-butyloxycarbonyl-L-Leu
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bromomethyl ketone derivative, utilized for purification procedure
1,10-phenanthroline
complete inhibition at 0.25 mM, reversible by Zn2+, not by other divalent cations, overview
1,10-phenanthroline
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the recombinant enzyme shows 18.8% relative activity in the presence of 1 mM 1,10-phenanthroline on hydrolysis of L-Leu-7-amido-4-methylcoumarin
1-butaneboronic acid
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binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
bestatin
complete inhibition at 0.1 mM, not reversible by divalent cations
bestatin
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strongly inhibited by bestatin, 20.5% relative activity in the presence of bestatin
bestatin
(2S)-2-[[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]amino]-4-methylpentanoic acid, inhibits HpM17AP and suppresses Helicobacter pylori growth, enzyme binding structure analysis from the crystal structures of HpM17AP and its complex with bestatin. The position of the D-phenylalanine moiety of the inhibitor with respect to the active-site metal ions, bicarbonate ion and with respect to other M17 aminopeptidases suggests that this residue binds to the S1 subsite of HpM17AP
bestatin
complete enzyme inhibition at 0.03 mM with substrate L-Leu-7-amido-4-methylcoumarin, in a murine model of tuberculosis, bestatin treatment reduces bacterial burden and lesion in the lungs of infected mice. Bestatin inhibits Mycobacterium tuberculosis growth in in vitro and ex vivo
bestatin
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reversible, slow, tight binding, transition state analog complex, Ki: 18 nM, stoichiometry of inhibition 1:1
Ca2+
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78% inhibition at 0.1 mM, 94% inhibition at 1 mM, 96% inhibition at 10 mM
dithiothreitol
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the recombinant enzyme shows 20.5% relative activity in the presence of 5 mM dithiothreitol on hydrolysis of L-Leu-7-amido-4-methylcoumarin
EDTA
complete inhibition at 1 mM, 50°C, 1 h, the activity can be restored by Co2+ and partially by Zn2+
EDTA
50% inhibition at 10 mM, reversible by divalent cations, best by Zn2+
L-leucine phosphonic acid
-
transition state inhibitor, binding structure and inhibition mechanism with Co/Zn-, Co/Co-, and Zn/Zn-enzyme
L-leucinethiol
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i.e. LeuSH, kinetic and spectroscopic characterization of the slow, tight-binding peptide inhibitor-enzyme complex, inhibition mechanism
n-valeramide
enzyme-inhibitor complex represents snapshot of proteolytic reaction between Michaelis-Menten and transition state
phenylmethylsulfonyl fluoride
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the recombinant enzyme shows 24.5% relative activity in the presence of 1 mM phenylmethylsulfonyl fluoride on hydrolysis of L-Leu-7-amido-4-methylcoumarin
Zn2+
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65% inhibition at 0.1 mM, 78% inhibition at 1 mM, 91% inhibition at 10 mM
additional information
no or poor inhibition by PMSF, E64, TLCK, pepstatin A, and leupeptin
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additional information
no inhibition by leupeptin and pepstatin A
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additional information
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no inhibition by leupeptin and pepstatin A
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additional information
the propeptides internally inhibits the enzyme in the 54 kDa zymogen in a cooperative inhibitory interaction
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additional information
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inhibited to a greater extend by D- than by L-hydroxamates of amino acids and aliphatic acids, pH-dependent
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additional information
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multiple inhibition study with substrate analogs and transition state analogs
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