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Literature summary for 3.4.11.20 extracted from

  • Ichishima, E.
    Aminopeptidase Ey (2004), Handbook of Proteolytic Enzymes (2nd Edition), 1, 294-296.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene apdE, DNA and amino acid sequence determination and analysis Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline complete inhibition at 2 mM Gallus gallus
betaine complete inhibition at 2 mM Gallus gallus
EDTA complete inhibition after dialysis for 24 h and 4°C against 1 mM EDTA Gallus gallus
OF 4949-II complete inhibition at 0.1 mM Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular plasma of egg yolk Gallus gallus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Gallus gallus
Cd2+ activates Gallus gallus
Co2+ activates Gallus gallus
Cu2+ activates Gallus gallus
Mn2+ activates Gallus gallus
additional information the enzyme is a metalloenzyme, the apoenzyme is inactive Gallus gallus
Ni2+ activates Gallus gallus
Zn2+ activates, required for activity and stability, zinc is bound by residues His386, His390, and Glu409 Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
N-Formyl-Met-Leu-Phe + H2O Gallus gallus
-
N-Formyl-Met + Leu-Phe
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
egg yolk plasma Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3083
-
purified enzyme Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Pro-Lys-Pro + H2O substance P fragment 1-4 Gallus gallus Arg + Pro-Lys-Pro
-
?
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
-
?
L-Leu-4-methylumbelliferyl + H2O
-
Gallus gallus L-leucine + 4-methylumbelliferol
-
?
L-Leu-4-nitroanilide + H2O
-
Gallus gallus L-leucine + 4-nitroaniline
-
?
Leu-enkephalin + H2O i.e. Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus Gallus gallus ?
-
?
Leu-Leu-Tyr + H2O
-
Gallus gallus Leu + Leu-Tyr
-
?
Leu-Pro-Leu-Arg-Phe-NH2 + H2O a chicken brain pentapeptide Gallus gallus Leu + Pro-Leu-Arg-Phe-NH2
-
?
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 ?
-
?
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 ?
-
?
N-Formyl-Met-Leu-Phe + H2O
-
Gallus gallus N-Formyl-Met + Leu-Phe
-
?
Pro-Phe-Gly-Lys + 2 H2O
-
Gallus gallus Pro + Phe + Gly-Lys
-
?

Subunits

Subunits Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Gallus gallus

pI Value

Organism Comment pI Value Maximum pI Value
Gallus gallus isoelectric focusing, holoenzyme
-
2.8
Gallus gallus isoelectric focusing, asialo enzyme form
-
4.4