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Literature summary for 3.4.11.22 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
Search for more literature for 3.4.11.22

Inhibitors

Inhibitors Comment Organism Structure
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
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
arginine hydroxamate competitive Tenebrio molitor
bestatin competitive Tenebrio molitor
crystal delta-endotoxin from Bacillus thuringiensis
-
 Tenebrio molitor
diethyldicarbonate inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation Tenebrio molitor
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
Methionine hydroxamate competitive Tenebrio molitor
additional information influence of inhibitors on each other, overview, no inhibition by 4-mercuribenzoate, isoamylalcohol and NaF Tenebrio molitor
Phenylglyoxal
-
 Tenebrio molitor
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]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metallopeptidase Tenebrio molitor

Organism

Organism UniProt Comment Textmining
Tenebrio molitor
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Tenebrio molitor

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
larva
-
 Tenebrio molitor
-
midgut
-
 Tenebrio molitor
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Range [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Tenebrio molitor

pH Range

pH Minimum pH Maximum Comment Organism
5 8.3 pH profile Tenebrio molitor

Ki Value [mM]

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