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Literature summary extracted from
- Aminopeptidase Ey (2004), Handbook of Proteolytic Enzymes (2nd Edition), 1, 294-296.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.20 | gene apdE, DNA and amino acid sequence determination and analysis | Gallus gallus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.20 | 1,10-phenanthroline | complete inhibition at 2 mM | Gallus gallus |  |
| 3.4.11.20 | betaine | complete inhibition at 2 mM | Gallus gallus | |
| 3.4.11.20 | EDTA | complete inhibition after dialysis for 24 h and 4°C against 1 mM EDTA | Gallus gallus | |
| 3.4.11.20 | OF 4949-II | complete inhibition at 0.1 mM | Gallus gallus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.11.20 | extracellular | plasma of egg yolk | Gallus gallus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.20 | Ca2+ | activates | Gallus gallus | |
| 3.4.11.20 | Cd2+ | activates | Gallus gallus | |
| 3.4.11.20 | Co2+ | activates | Gallus gallus | |
| 3.4.11.20 | Cu2+ | activates | Gallus gallus | |
| 3.4.11.20 | Mn2+ | activates | Gallus gallus | |
| 3.4.11.20 | additional information | the enzyme is a metalloenzyme, the apoenzyme is inactive | Gallus gallus | |
| 3.4.11.20 | Ni2+ | activates | Gallus gallus | |
| 3.4.11.20 | Zn2+ | activates, required for activity and stability, zinc is bound by residues His386, His390, and Glu409 | Gallus gallus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.20 | additional information | Gallus gallus | the enzyme functiones in regulation of hormone function and thus is involved in diverse biological processes, it offers a biodefense against the infectious microbial product N-formyl-peptide | ? | - |
? | |
| 3.4.11.20 | N-Formyl-Met-Leu-Phe + H2O | Gallus gallus | - |
N-Formyl-Met + Leu-Phe | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.20 | Gallus gallus | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.11.20 | glycoprotein | - |
Gallus gallus |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.20 | to homogeneity | Gallus gallus |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.11.20 | differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position | Glu387 is an essential catalytic residue | Gallus gallus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.11.20 | egg yolk | plasma | Gallus gallus | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.20 | 3083 | - |
purified enzyme | Gallus gallus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.20 | Arg-Pro-Lys-Pro + H2O | substance P fragment 1-4 | Gallus gallus | Arg + Pro-Lys-Pro | - |
? | |
| 3.4.11.20 | cholecystokinin octapeptide + H2O | i.e. Asp-tyrosyl sulfate-Met-Gly-Trp-Met-Asp-Phe-NH2 | Gallus gallus | tyrosine sulfate + Asp + Met + Gly + Trp + Met-Asp-Phe-NH2 | - |
? | |
| 3.4.11.20 | L-Leu-4-methylumbelliferyl + H2O | - |
Gallus gallus | L-leucine + 4-methylumbelliferol | - |
? | |
| 3.4.11.20 | L-Leu-4-nitroanilide + H2O | - |
Gallus gallus | L-leucine + 4-nitroaniline | - |
? | |
| 3.4.11.20 | Leu-enkephalin + H2O | i.e. Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus | Gallus gallus | ? | - |
? | |
| 3.4.11.20 | Leu-Leu-Tyr + H2O | - |
Gallus gallus | Leu + Leu-Tyr | - |
? | |
| 3.4.11.20 | Leu-Pro-Leu-Arg-Phe-NH2 + H2O | a chicken brain pentapeptide | Gallus gallus | Leu + Pro-Leu-Arg-Phe-NH2 | - |
? | |
| 3.4.11.20 | additional information | the enzyme functiones in regulation of hormone function and thus is involved in diverse biological processes, it offers a biodefense against the infectious microbial product N-formyl-peptide | Gallus gallus | ? | - |
? | |
| 3.4.11.20 | additional information | the enzyme has a broad specificity for N-terminal amino acids residues at the P1 position of substrates, it degrades hydrophobic, basic, and acidic amino acids including proline, no activity with substance P and melanocyte-stimulating hormone release-inhibiting factor, i.e. Pro-Leu-Gly-NH2 | Gallus gallus | ? | - |
? | |
| 3.4.11.20 | N-Formyl-Met-Leu-Phe + H2O | - |
Gallus gallus | N-Formyl-Met + Leu-Phe | - |
? | |
| 3.4.11.20 | Pro-Phe-Gly-Lys + 2 H2O | - |
Gallus gallus | Pro + Phe + Gly-Lys | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.20 | More | the native enzyme contains 14% alpha helix and 68% beta-sheet, while the apoenzyme contains only 6% alpha helix, and 70% beta-sheet, tertiary structure | Gallus gallus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.20 | 7.5 | - |
- |
Gallus gallus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.11.20 | Gallus gallus | isoelectric focusing, holoenzyme | - |
2.8 |
| 3.4.11.20 | Gallus gallus | isoelectric focusing, asialo enzyme form | - |
4.4 |
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