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Information on EC 3.4.11.10 - bacterial leucyl aminopeptidase and Organism(s) Helicobacter pylori and UniProt Accession O25294

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.10 bacterial leucyl aminopeptidase
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This record set is specific for:
Helicobacter pylori
UNIPROT: O25294 not found.
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Word Map
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The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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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
Synonyms
cgase, ap-ii, cysteinylglycinase, hpm17ap, fglap, lapii, mtlap, m17 aminopeptidase, thermostable leucine aminopeptidase, leucine apn, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bacterial M17 aminopeptidase
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M17 aminopeptidase
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Aeromonas proteolytica aminopeptidase
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-
-
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Leucyl aminopeptidase
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ribosomal-bound aminopeptidase
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-67-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-arginine + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
-
-
?
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-cysteine + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
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-
-
?
L-leucyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-leucine + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
-
-
?
L-methionyl 7-amido-4-carbamoylmethylcoumarin + H2O
L-methionine + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
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-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
the sodium ion is coordinated by the main-chain carbonyl oxygen atoms of A461, G462, Y465 and three water molecules in an octahedral geometry
Zn2+
two active-site positively charged zinc ions are coordinated by negatively charged side-chain oxygen atoms of three aspartate residues (D263, D281, D340) and one glutamate residue (E342), the side-chain nitrogen atom of K258 and two water molecules in a distorted octahedral coordination geometry
Co2+
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highly activating, about 5fold at 1-10 mM
Mg2+
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activates 2.9fold at 1 mM, 3.7fold at 10 mM
Mn2+
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highly activating, 5.6fold at 1-10 mM
Ni2+
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activates 3.5fold at 1 mM, 3.8fold at 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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inhibits the enzyme activity and cell growth
Ca2+
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78% inhibition at 0.1 mM, 94% inhibition at 1 mM, 96% inhibition at 10 mM
EDTA
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97% inhibition at 0.1 mM
Zn2+
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65% inhibition at 0.1 mM, 78% inhibition at 1 mM, 91% inhibition at 10 mM
additional information
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no inhibition by PMSF
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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recombinant LAP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
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pH profile, about 40% of maximal activity at pH 5.5 and pH 10.0, rapid decline of activity at pH 5.0, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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recombinant LAP
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 100
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temperature profile, about 60% of maximal activity at 15°C and 100°C, recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Campylobacter pylori
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the M17 aminopeptidase from the carcinogenic gastric bacterium Helicobacter pylori (HpM17AP) is an important housekeeping enzyme involved in catabolism of endogenous and exogenous peptides. It is implicated in Helicobacter pylori defence against the human innate immune response and in the mechanism of metronidazole resistance
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
260000
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gel filtration
340000
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recombinant enzyme, gel filtration
55000
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6 * 55000, recombinant LAP, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
LAP in complex with bestatin is crystallized to 2.8 A resolution using the hanging-drop vapour-diffusion method
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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gene LAP, DNA and amino acid sequence determination and analysis, functional expression of His-tagged enzyme in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
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the enzyme is a target for development of anti-Helicobacter pylori agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dong, L.; Cheng, N.; Wang, M.W.; Zhang, J.; Shu, C.; Zhu, D.X.
The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme
Microbiology
151
2017-2023
2005
Helicobacter pylori
Manually annotated by BRENDA team
Modak, J.K.; Roujeinikova, A.
Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori leucyl aminopeptidase-bestatin complex
Acta Crystallogr. Sect. F
69
1011-1014
2013
Helicobacter pylori
Manually annotated by BRENDA team
Modak, J.K.; Rut, W.; Wijeyewickrema, L.C.; Pike, R.N.; Drag, M.; Roujeinikova, A.
Structural basis for substrate specificity of Helicobacter pylori M17 aminopeptidase
Biochimie
121
60-71
2016
Helicobacter pylori (O25294), Helicobacter pylori, Helicobacter pylori 26695 (O25294), Helicobacter pylori ATCC 700392 (O25294)
Manually annotated by BRENDA team