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Literature summary extracted from

  • Cristofoletti, P.T.; Terra, W.R.
    The role of amino acid residues in the active site of a midgut microvillar aminopeptidase from the beetle Tenebrio molitor (2000), Biochim. Biophys. Acta, 1479, 185-195.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.22 1,10-phenanthroline half-maximal inhibition at 1.8 mM, competitive and reversible inhibition is reversed by ZnCl2, increases 20fold the inhibition by EDTA Tenebrio molitor
3.4.11.22 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide inactivation by modification of pK 5.8 carboxylate, presence arginine hydroxamate decreases inhibitory potency, hydroxylamine does not recover enzyme activity Tenebrio molitor
3.4.11.22 arginine hydroxamate competitive Tenebrio molitor
3.4.11.22 bestatin competitive Tenebrio molitor
3.4.11.22 crystal delta-endotoxin from Bacillus thuringiensis
-
 Tenebrio molitor
3.4.11.22 diethyldicarbonate inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation Tenebrio molitor
3.4.11.22 EDTA inactivation, is affected by pH and temperature, metal binding of at least one deprotonated imidazole group is involved, presence of arginine hydroxamate decreases inhibitory potency, increased by 1,10-phenanthroline Tenebrio molitor
3.4.11.22 Methionine hydroxamate competitive Tenebrio molitor
3.4.11.22 additional information influence of inhibitors on each other, overview, no inhibition by 4-mercuribenzoate, isoamylalcohol and NaF Tenebrio molitor
3.4.11.22 Phenylglyoxal
-
 Tenebrio molitor
3.4.11.22 Tetranitromethane changes the Km of the enzyme without affecting Vmax by modifying a phenol group, presence arginine hydroxamate decreases inhibitory potency Tenebrio molitor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.22 additional information
-
 additional information kinetics and thermodynamics Tenebrio molitor

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.22 membrane
-
 Tenebrio molitor 16020
-
3.4.11.22 microvillus
-
 Tenebrio molitor 5902
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.22 additional information metallopeptidase Tenebrio molitor

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.22 Tenebrio molitor
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.22
-
 Tenebrio molitor

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.11.22 Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates catalysis depends on a catalytic metal, a carboxylate and a protonated imidazole group, whereas substrate binding requires one phenol and one carboxylate group Tenebrio molitor
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.22 larva
-
 Tenebrio molitor
-
3.4.11.22 midgut
-
 Tenebrio molitor
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.22 Leu-4-nitroanilide + H2O
-
 Tenebrio molitor Leu + 4-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.22 Aminopeptidase III
-
 Tenebrio molitor
3.4.11.22 Aminopeptidase yscI
-
 Tenebrio molitor
3.4.11.22 Leucine aminopeptidase IV
-
 Tenebrio molitor
3.4.11.22 More enzyme belongs to the peptidase family M18 Tenebrio molitor
3.4.11.22 Yeast aminopeptidase I
-
 Tenebrio molitor

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.11.22 10 45
-
 Tenebrio molitor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.22 8
-
-
 Tenebrio molitor

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.11.22 5 8.3 pH profile Tenebrio molitor

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.11.22 additional information
-
 additional information inhibition kinetics Tenebrio molitor
3.4.11.22 0.6
-
 arginine hydroxamate pH 7.8, 30°C Tenebrio molitor
3.4.11.22 0.7
-
 EDTA pH 7.8, 37°C, in presence of 1,10-phenanthroline Tenebrio molitor
3.4.11.22 1.2
-
 1,10-phenanthroline pH 7.8, 37°C Tenebrio molitor