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Information on EC 3.4.11.10 - bacterial leucyl aminopeptidase and Organism(s) Pseudomonas putida and UniProt Accession O86436

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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:
Pseudomonas putida
UNIPROT: O86436 not found.
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The taxonomic range for the selected organisms is: Pseudomonas putida
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, fglap, hpm17ap, lapii, mtlap, m17 aminopeptidase, thermostable leucine aminopeptidase, rlap55, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
leucine aminopeptidase
-
Aeromonas proteolytica aminopeptidase
-
-
-
-
bacterial leucine aminopeptidase
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ribosomal-bound aminopeptidase
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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
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
at pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2. Mn2+ has a significant activation effect when bound to site 1 of ppLAP
Zn2+
LAP is zinc-dependent. At pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2
additional information
ppLAP requires the presence of divalent metal ions for its activity, in particular Zn2+ and/or Mn2+. At pH 5.2, the active site of ppLAP is highly disordered and metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bestatin
binding structure and comparison, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is inactive at low pH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMPA_PSEPU
497
0
52469
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
270000
recombinant enzyme, gel filtration
50000
-
8 * 50000, about
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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8 * 50000, about
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by cation exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
LAP is an important enzyme for the industrial production of enantiomerically pure amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Kale, A.; Pijning, T.; Sonke, T.; Dijkstra, B.W.; Thunnissen, A.M.
Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity
J. Mol. Biol.
398
703-714
2010
Pseudomonas putida (O86436)
Manually annotated by BRENDA team