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 |
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 |
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 | - |
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 |
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 |
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 | ? | - |
? |
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 | - |
- |
- |
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 | - |
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 | ? | - |
? |
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 |
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 |