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Literature summary for 3.4.11.2 extracted from

  • Jankiewicz, U.; Bielawski, W.
    The properties and functions of bacterial aminopeptidases (2003), Acta Microbiol. Pol., 52, 217-231.
    View publication on PubMed
Search for more literature for 3.4.11.2

Activating Compound

Activating Compound Comment Organism Structure
additional information 4fold up-regulation in case of oxygen or phosphorus deficit, but not in case of nitrogen or carbon deficit Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
dipeptides inhibit the enzyme at high concentration in the medium Lactococcus lactis
additional information detection of en endogenous inhibior Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol the enzyme is associated to the plasmam membrane at the cytosolic side Pseudomonas aeruginosa 5829
-
intracellular
-
 Pseudomonas fluorescens 5622
-
plasma membrane the enzyme is associated to the plasmam membrane at the cytosolic side Pseudomonas aeruginosa 5886
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Pseudomonas aeruginosa aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Lactococcus lactis aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Streptococcus thermophilus aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Lactobacillus delbrueckii aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Latilactobacillus curvatus aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
additional information Pseudomonas fluorescens the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Lactobacillus delbrueckii
-
-
-
Lactococcus lactis
-
-
-
Latilactobacillus curvatus
-
-
-
Pseudomonas aeruginosa
-
-
-
Pseudomonas fluorescens
-
 strain ATCC 948
-
Streptococcus thermophilus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information enzyme expression during whole life cycle, 4fold up-regulation in case of oxygen or phosphorus deficit, but not in case of nitrogen or carbon deficit Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information aminopeptidase regulation mechanisms and biological functions, overview Escherichia coli ?
-
 ?
additional information aminopeptidase regulation mechanisms and biological functions, overview Pseudomonas aeruginosa ?
-
 ?
additional information aminopeptidase regulation mechanisms and biological functions, overview Lactococcus lactis ?
-
 ?
additional information aminopeptidase regulation mechanisms and biological functions, overview Streptococcus thermophilus ?
-
 ?
additional information aminopeptidase regulation mechanisms and biological functions, overview Lactobacillus delbrueckii ?
-
 ?
additional information aminopeptidase regulation mechanisms and biological functions, overview Latilactobacillus curvatus ?
-
 ?
additional information the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview Pseudomonas fluorescens ?
-
 ?
additional information broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues Lactococcus lactis ?
-
 ?
additional information broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues Streptococcus thermophilus ?
-
 ?
additional information broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues Lactobacillus delbrueckii ?
-
 ?
additional information broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues Latilactobacillus curvatus ?
-
 ?
additional information the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Ala, Arg, Lys or Leu residues Pseudomonas fluorescens ?
-
 ?
additional information the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Ala, Arg, Lys or Leu residues Pseudomonas aeruginosa ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Escherichia coli
monomer
-
 Pseudomonas fluorescens
monomer
-
 Pseudomonas aeruginosa
monomer
-
 Lactococcus lactis
monomer
-
 Streptococcus thermophilus
monomer
-
 Lactobacillus delbrueckii
monomer
-
 Latilactobacillus curvatus

Synonyms

Synonyms Comment Organism
aminopeptidase N
-
 Escherichia coli
aminopeptidase N
-
 Pseudomonas fluorescens
aminopeptidase N
-
 Pseudomonas aeruginosa
aminopeptidase N
-
 Lactococcus lactis
aminopeptidase N
-
 Streptococcus thermophilus
aminopeptidase N
-
 Lactobacillus delbrueckii
aminopeptidase N
-
 Latilactobacillus curvatus