Any feedback?
Literature summary extracted from
- Leucyl aminopeptidase PepA (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds), 1, 905-910.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.10 | overexpression | Escherichia coli |
| 3.4.11.10 | overexpression in Escherichia coli | Pseudomonas aeruginosa |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.11.10 | purified PepA, X-ray diffraction structure determination and analysis at 2.5 A resolution | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.11.10 | E354A | site-directed mutagenesis, inactive mutant | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.10 | bestatin | - |
Pseudomonas aeruginosa |  |
| 3.4.11.10 | EDTA | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.10 | Cd2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.11.10 | Cd2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Escherichia coli | |
| 3.4.11.10 | Co2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.11.10 | Co2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Escherichia coli | |
| 3.4.11.10 | Mg2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.11.10 | Mg2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site | Escherichia coli | |
| 3.4.11.10 | Mn2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.11.10 | Mn2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site | Escherichia coli | |
| 3.4.11.10 | Ni2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.11.10 | Ni2+ | metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+ | Escherichia coli | |
| 3.4.11.10 | Zn2+ | 2 ions bound per enzyme molecule, binding to Glu354 | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.10 | 54879 | - |
6 * 54879, structure analysis and sequence calculation, three-dimensional structure modelling with C-terminal catalytic domain | Escherichia coli |
| 3.4.11.10 | 323000 | - |
PepA in solution | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.10 | albomycin + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | PepA activates albomycin | ? | - |
? | |
| 3.4.11.10 | Cys-Gly + H2O | Escherichia coli | glutathione-derived substrate, PepA is involved in the cysteine salvage pathway | Cys + Gly | - |
? | |
| 3.4.11.10 | additional information | Escherichia coli | biological functions overview, the enzyme functions in the final steps of protein turnover during starvation and in degradation of abnormal proteins, the enzyme binds DNA and is active in both transcriptional regulation and site-specific recombination, and is involved in regulation of the carAB operon | ? | - |
? | |
| 3.4.11.10 | additional information | Pseudomonas aeruginosa | biological functions overview, the enzyme is involved in control of signal transduction leading to alginate expression | ? | - |
? | |
| 3.4.11.10 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium | biological functions overview, the enzyme is involved in regulation of Xer sites-specific recombination | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.10 | Escherichia coli | - |
gene xerB | - |
| 3.4.11.10 | Pseudomonas aeruginosa | - |
gene phpA | - |
| 3.4.11.10 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
gene pepA | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.10 | native enzyme from crude cell extract, and recombinant enzyme from overexpressing cells, by anion exchange and hydrophobic interaction chromatography, and gel filtration | Escherichia coli |
| 3.4.11.10 | recombinant enzyme partially from Escherichia coli | Pseudomonas aeruginosa |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.11.10 | Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. | Glu354 is essential for Zn2+-binding and catalytic activity, Arg356 is involved in catalysis acting as a general base that accepts a proton and activates the water nucleophile, other active site residues are Lys270, Glu354, ASp352, Lys282, Asp275, and Asp293, mechanism | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.10 | albomycin + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 3.4.11.10 | albomycin + H2O | PepA activates albomycin | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 3.4.11.10 | Cys-Gly + H2O | - |
Escherichia coli | Cys + Gly | - |
? | |
| 3.4.11.10 | Cys-Gly + H2O | glutathione-derived substrate, PepA is involved in the cysteine salvage pathway | Escherichia coli | Cys + Gly | - |
? | |
| 3.4.11.10 | L-Leu-4-nitroanilide + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | L-Leu + 4-nitroaniline | - |
? | |
| 3.4.11.10 | L-Leu-4-nitroanilide + H2O | - |
Pseudomonas aeruginosa | L-Leu + 4-nitroaniline | - |
? | |
| 3.4.11.10 | L-Leu-4-nitroanilide + H2O | preferably with Mn2+ | Escherichia coli | L-Leu + 4-nitroaniline | - |
? | |
| 3.4.11.10 | L-Pro-4-nitroanilide + H2O | - |
Escherichia coli | L-Pro + 4-nitroaniline | - |
? | |
| 3.4.11.10 | additional information | biological functions overview, the enzyme functions in the final steps of protein turnover during starvation and in degradation of abnormal proteins, the enzyme binds DNA and is active in both transcriptional regulation and site-specific recombination, and is involved in regulation of the carAB operon | Escherichia coli | ? | - |
? | |
| 3.4.11.10 | additional information | biological functions overview, the enzyme is involved in control of signal transduction leading to alginate expression | Pseudomonas aeruginosa | ? | - |
? | |
| 3.4.11.10 | additional information | biological functions overview, the enzyme is involved in regulation of Xer sites-specific recombination | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 3.4.11.10 | additional information | broad-range specificity, the enzyme binds DNA and is active in both transcriptional regulation and site-specific recombination, the enzyme prefers tripeptide substrates with N-terminal leucyl- or methionyl-residues, dipeptides or C3-C6 peptides are also cleaved but more slowly, no activity with albomycin | Escherichia coli | ? | - |
? | |
| 3.4.11.10 | additional information | broad-range specificity, the enzyme prefers tripeptide substrates with N-terminal leucyl- or methionyl-residues, dipeptides or C3-C6 peptides are also cleaved but more slowly, no activity with peptides with proline at the second position | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.10 | hexamer | 6 * 54879, structure analysis and sequence calculation, three-dimensional structure modelling with C-terminal catalytic domain | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.10 | aminopeptidase A (bacteria) | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.11.10 | aminopeptidase A (bacteria) | - |
Escherichia coli |
| 3.4.11.10 | aminopeptidase A (bacteria) | - |
Pseudomonas aeruginosa |
| 3.4.11.10 | PepA | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.11.10 | PepA | - |
Escherichia coli |
| 3.4.11.10 | Peptidase A | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.11.10 | PhpA | - |
Pseudomonas aeruginosa |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.10 | additional information | - |
the enzyme is heat-stable | Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.11.10 | additional information | - |
the enzyme is heat-stable | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
