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Literature summary extracted from

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

Activating Compound

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.2 dipeptides inhibit the enzyme at high concentration in the medium Lactococcus lactis
3.4.11.2 additional information detection of en endogenous inhibior Escherichia coli
3.4.11.10 EDTA complete inactivation, reversible by Zn2+, Co2+, Ni2+, or Cu2+ Vibrio proteolyticus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.2 cytosol the enzyme is associated to the plasmam membrane at the cytosolic side Pseudomonas aeruginosa 5829
-
3.4.11.2 intracellular
-
 Pseudomonas fluorescens 5622
-
3.4.11.2 plasma membrane the enzyme is associated to the plasmam membrane at the cytosolic side Pseudomonas aeruginosa 5886
-
3.4.11.10 extracellular
-
 Pseudomonas aeruginosa
-
-
3.4.11.10 extracellular
-
 Vibrio proteolyticus
-
-
3.4.11.10 intracellular
-
 Salmonella enterica subsp. enterica serovar Typhimurium 5622
-
3.4.11.10 intracellular
-
 Escherichia coli 5622
-
3.4.11.10 intracellular
-
 Pseudomonas aeruginosa 5622
-
3.4.11.10 intracellular
-
 Vibrio proteolyticus 5622
-
3.4.11.10 plasma membrane the enzyme is asscoiated to the internal membrane surface Lactococcus sp. 5886
-
3.4.11.24 extracellular
-
 Streptomyces griseus
-
-
3.4.11.24 intracellular
-
 Streptomyces griseus 5622
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.10 additional information metallopeptidase, the kind of bound metal ion determines the substrate specificity Salmonella enterica subsp. enterica serovar Typhimurium
3.4.11.10 additional information metallopeptidase, the kind of bound metal ion determines the substrate specificity Escherichia coli
3.4.11.10 additional information metallopeptidase, the kind of bound metal ion determines the substrate specificity Vibrio proteolyticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.10 additional information
-
 extracellular enzymes show a low MW of 20-30 kDa Pseudomonas aeruginosa
3.4.11.10 additional information
-
 extracellular enzymes show a low MW of 20-30 kDa Vibrio proteolyticus
3.4.11.10 18000
-
 12 * 18000 Brevibacterium linens
3.4.11.10 47000
-
 x * 47000 + x * 50000 Mycoplasma salivarium
3.4.11.10 50000
-
 8 * 50000, about Pseudomonas putida
3.4.11.10 50000
-
 x * 47000 + x * 50000 Mycoplasma salivarium
3.4.11.10 55000
-
 6 * 55000 Escherichia coli
3.4.11.10 400000
-
-
 Pseudomonas putida
3.4.11.24 additional information
-
 extracellular enzymes show a low MW of 20-30 kDa Streptomyces griseus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.2 additional information Escherichia coli aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Pseudomonas aeruginosa aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Lactococcus lactis aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Streptococcus thermophilus aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Lactobacillus delbrueckii aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Latilactobacillus curvatus aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.2 additional information Pseudomonas fluorescens the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview ?
-
 ?
3.4.11.10 additional information Salmonella enterica subsp. enterica serovar Typhimurium aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Escherichia coli aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Pseudomonas aeruginosa aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Pseudomonas putida aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Brevibacterium linens aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Vibrio proteolyticus aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Mycoplasma salivarium aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Lactococcus sp. the enzyme is involved in transport and degradation of extracellular peptides, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.10 additional information Brevibacterium linens SR3 aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?
3.4.11.24 additional information Streptomyces griseus aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.2 Escherichia coli
-
-
-
3.4.11.2 Lactobacillus delbrueckii
-
-
-
3.4.11.2 Lactococcus lactis
-
-
-
3.4.11.2 Latilactobacillus curvatus
-
-
-
3.4.11.2 Pseudomonas aeruginosa
-
-
-
3.4.11.2 Pseudomonas fluorescens
-
 strain ATCC 948
-
3.4.11.2 Streptococcus thermophilus
-
-
-
3.4.11.10 Brevibacterium linens
-
-
-
3.4.11.10 Brevibacterium linens SR3
-
-
-
3.4.11.10 Escherichia coli
-
-
-
3.4.11.10 Lactococcus sp.
-
-
-
3.4.11.10 Mycoplasma salivarium
-
-
-
3.4.11.10 Pseudomonas aeruginosa
-
-
-
3.4.11.10 Pseudomonas putida
-
-
-
3.4.11.10 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
3.4.11.10 Vibrio proteolyticus
-
 formerly Aeromonas proteolytica
-
3.4.11.24 Streptomyces griseus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.2 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Escherichia coli ?
-
 ?
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Pseudomonas aeruginosa ?
-
 ?
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Lactococcus lactis ?
-
 ?
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Streptococcus thermophilus ?
-
 ?
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Lactobacillus delbrueckii ?
-
 ?
3.4.11.2 additional information aminopeptidase regulation mechanisms and biological functions, overview Latilactobacillus curvatus ?
-
 ?
3.4.11.2 additional information the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview Pseudomonas fluorescens ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.2 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 ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Escherichia coli ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Pseudomonas aeruginosa ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Pseudomonas putida ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Brevibacterium linens ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Vibrio proteolyticus ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Mycoplasma salivarium ?
-
 ?
3.4.11.10 additional information the enzyme is involved in transport and degradation of extracellular peptides, and are important in uptake of nutrients, regulation, overview Lactococcus sp. ?
-
 ?
3.4.11.10 additional information the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
3.4.11.10 additional information the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position Escherichia coli ?
-
 ?
3.4.11.10 additional information the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position Pseudomonas aeruginosa ?
-
 ?
3.4.11.10 additional information the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position Vibrio proteolyticus ?
-
 ?
3.4.11.10 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Brevibacterium linens SR3 ?
-
 ?
3.4.11.24 additional information aminopeptidases are involved in peptides processing and degradation, and are important in uptake of nutrients, regulation, overview Streptomyces griseus ?
-
 ?
3.4.11.24 additional information the enzyme shows broad substrate specificity preferring N-terminal Leu or Met and Phe, but is not able to hydrolyse peptide substrates bonds with formed by acidic amino acids in the P1 position or proline in the P1 or P1' position Streptomyces griseus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.2 monomer
-
 Escherichia coli
3.4.11.2 monomer
-
 Pseudomonas fluorescens
3.4.11.2 monomer
-
 Pseudomonas aeruginosa
3.4.11.2 monomer
-
 Lactococcus lactis
3.4.11.2 monomer
-
 Streptococcus thermophilus
3.4.11.2 monomer
-
 Lactobacillus delbrueckii
3.4.11.2 monomer
-
 Latilactobacillus curvatus
3.4.11.10 ? x * 47000 + x * 50000 Mycoplasma salivarium
3.4.11.10 dodecamer 12 * 18000 Brevibacterium linens
3.4.11.10 hexamer 6 * 55000 Escherichia coli
3.4.11.10 octamer 8 * 50000, about Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
3.4.11.2 aminopeptidase N
-
 Escherichia coli
3.4.11.2 aminopeptidase N
-
 Pseudomonas fluorescens
3.4.11.2 aminopeptidase N
-
 Pseudomonas aeruginosa
3.4.11.2 aminopeptidase N
-
 Lactococcus lactis
3.4.11.2 aminopeptidase N
-
 Streptococcus thermophilus
3.4.11.2 aminopeptidase N
-
 Lactobacillus delbrueckii
3.4.11.2 aminopeptidase N
-
 Latilactobacillus curvatus
3.4.11.10 aminopeptidase A
-
 Escherichia coli
3.4.11.10 aminopeptidase A
-
 Lactococcus sp.
3.4.11.10 bacterial leucine aminopeptidase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.4.11.10 bacterial leucine aminopeptidase
-
 Escherichia coli
3.4.11.10 bacterial leucine aminopeptidase
-
 Pseudomonas aeruginosa
3.4.11.10 bacterial leucine aminopeptidase
-
 Pseudomonas putida
3.4.11.10 bacterial leucine aminopeptidase
-
 Brevibacterium linens
3.4.11.10 bacterial leucine aminopeptidase
-
 Vibrio proteolyticus
3.4.11.10 PepA
-
 Escherichia coli
3.4.11.24 bacterial leucine aminopeptidase
-
 Streptomyces griseus