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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

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.10 bacterial leucyl aminopeptidase

Crystallization

Crystallization on EC 3.4.11.10 - bacterial leucyl aminopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme with or without Zn2+, hanging drop vapour diffusion method, method screening, 0.006 ml protein solution against 1 ml reservoir solution, which contains2.0-2.5 M ammonium sulfate, 14-60 days, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution, multiwavelength anomalous diffraction
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crystallization at pH 8.0 of enzyme in high salt Tris buffer against low salt concentration, X-ray diffraction crystal structure determination and analysis at 2.5 A resolution
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purified PepA, X-ray diffraction structure determination and analysis at 2.5 A resolution
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LAP in complex with bestatin is crystallized to 2.8 A resolution using the hanging-drop vapour-diffusion method
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purified enzyme free and in complex with inhibitor bestatin, enzyme bound with Zn2+ and Na+, hanging drop vapour-diffusion method, mixing of 0.002 ml of 11.2 mg/ml protein solution with 0.002 ml of reservoir solution containing 11% w/v PEG 3350 and 100 mM sodium formate, pH 7.0, and equilibration against reservoir solution, crystals of HpM17AP-bestatin complex are obtained by using 5.6 mg/ml protein, 1 mM bestatin and the reservoir solution containing 12% w/v PEG 2000 and 100 mM sodium formate, pH 7.0, 19°C, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, molecular replacement using the structure of LAP from Pseudomonas putida (PDB ID 3h8g) as a search model
purified enzyme in complex with inhibitor bestatin at pH 5.2 and pH 9.5, hanging drop vapour diffusion, 8 mg/ml protein in 20 mM HEPES–KOH, pH 8.0, 1 mM DTT, is mixed with 11% w/v PEG 8000, 0.2 M sodium formate, 0.1 M Mes–NaOH, pH 5.2, 1 mM NaN3 at 5°C, or 4 mg/ml protein solution is mixed with 15% w/v PEG 1500, 0.1 M propionic acid, cacodylate, bis-Tris propane cocktail buffer, pH 9.5 at 23°C, three days, X-ray diffraction structure determination and analysis at 1.5-2.75 A resolution, modelling
10 mg/ml purified enzyme, complexed with inhibitor L-leucinephosphonic acid from a 4fold molar excess, with precipitation solution containing Tris, pH 8.0, 10 mM KSCN, 0.4 M NaCl, 4 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
16 mg/ml enzyme complexed with inhibitory Tris, in 10 mM Tris, pH 8.0, 10 mM KSCN, 0.4 NaCl, vapour diffusion method, with precipitant solution containing 100 mM Tris, pH 8.0, 100 mM KSCN, 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution
analysis of crystal structures of free Zn-enzyme, and Zn-enyme bound to different inhibitors, complex optimizations, overview
free Zn-enzyme or enzyme in complex with synthetic inhibitor 4-iodo-D-phenylalanine hydroxamate, X-ray diffraction structure determination and analysis at 1.8 A resolution
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hanging drop vapour diffusion method, aminopeptidase in 10 mM Tris buffer, pH 8.0, containing 10 mM KSCN and 400 mM NaCl is equilibrated with 100 mM Tris buffer, pH 8.0, containing 100 mM KSCN and 4.5 M NaCl, at 19°C
hanging drop vapour diffusion method, at 25°C
purified enzyme in complex Tris, 16 mg/ml in 10 mM Tris, pH 8.0, 10 mM KSCN, and 0.4 M NaCl, hanging drop vapour diffusion method, precipitation solution contains 100 mM Tris, pH 8.0, 100 mM KSCN, and 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling
purified recombinant E151H mutant holoenzyme, 15 mg/ml protein in 10 mM HEPES, pH 7.2, 10 mM KSCN, and 0.4 M NaCl,vapour diffusion mehtod, the precipitation solution contains 100 mM HEPES, pH 7.2, 100 mM KSCN, and 4.5 M NaCl, 2-3 days, X-ray diffraction structure determination and analysis at 1.9 A resolution and room temperature
structure of enzyme-inhibitor complex reported
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X-ray crystal structure of an aminopeptidase-L-leucyl-L-leucyl-L-leucine complex, sitting-drop method
X-ray study, 45% solvent content estimated
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purified recombinant His-tagged enzyme, sitting drop vapour diffusion method, 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 1 M NaCl, 3 mM 2-mercaptoethanol, 40 mM imidazole and 20% v/v glycerol, is mixed with precipitant solution containing 0.02 M CaCl2, 0.1 M sodium acetate, pH 4.6-5.0, and 15%, 20% or 40% v/v MPD, different conditions resulting in different crystal forms, X-ray diffraction structure determination and analysis at 2.6 A resolution
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