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Literature summary for 3.4.24.55 extracted from

  • Fricke, B.; Betz, R.; Friebe, S.
    A periplasmic insulin-cleaving proteinase (ICP) from Acinetobacter calcoaceticus sharing properties with protease III from Escherichia coli and IDE from eucaryotes (1995), J. Basic Microbiol., 35, 21-31.
    View publication on PubMed
Search for more literature for 3.4.24.55

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline Co2+, and to a lesser extent but at lower metal ion concentration Zn2+ restores activity Acinetobacter calcoaceticus
1,10-phenanthroline Co2+, and to a lesser extent but at lower metal ion concentration Zn2+ restores activity Escherichia coli
antipain
-
 Acinetobacter calcoaceticus
chymostatin
-
 Acinetobacter calcoaceticus
Co2+
-
 Acinetobacter calcoaceticus
Co2+
-
 Escherichia coli
DTT
-
 Acinetobacter calcoaceticus
DTT
-
 Escherichia coli
EDTA Co2+, and to a lesser extent but at lower metal ion concentration Zn2+ restores activity Acinetobacter calcoaceticus
EDTA Co2+, and to a lesser extent but at lower metal ion concentration Zn2+ restores activity Escherichia coli
PCMB
-
 Acinetobacter calcoaceticus
phosphoramidon
-
 Acinetobacter calcoaceticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000105
-
 Insulin
-
 Acinetobacter calcoaceticus

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-
periplasm
-
 Acinetobacter calcoaceticus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ reactivation after inhibition with chelating agents Escherichia coli
Co2+ reactivation after inhibition with chelating agents Acinetobacter calcoaceticus
Zn2+ most effective metal ion in reactivation after inhibition by chelating agent Escherichia coli
Zn2+ most effective metal ion in reactivation after inhibition by chelating agent Acinetobacter calcoaceticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
107000
-
 1 * 107000, Acinetobacter calcoaceticus, SDS-PAGE Escherichia coli
107000
-
 1 * 107000, Acinetobacter calcoaceticus, SDS-PAGE Acinetobacter calcoaceticus

Organism

Organism UniProt Comment Textmining
Acinetobacter calcoaceticus
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
similar enzyme Acinetobacter calcoaceticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glucagon + H2O
-
 Escherichia coli ?
-
 ?
Glucagon + H2O
-
 Acinetobacter calcoaceticus ?
-
 ?
Insulin + H2O
-
 Escherichia coli Hydrolyzed insulin
-
 ?
Insulin + H2O
-
 Acinetobacter calcoaceticus Hydrolyzed insulin
-
 ?
Insulin B-chain + H2O
-
 Escherichia coli ?
-
 ?
Insulin B-chain + H2O cleavage sites are Asn3-Gln4, His10-Leu11, Ala14-Leu15, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, Phe25-Tyr26, the enzyme shares one of the only two cleavage sites with pitrilysin and 4 sites with insulin-destroying insulinase (EC 3.4.24.56) Acinetobacter calcoaceticus ?
-
 ?
additional information
-
 Escherichia coli ?
-
 ?
additional information prefers the cleavage of small polypeptides to the cleavage of proteins, inactive against synthetic amino acid derivatives of subtilisin, thermolysin, trypsin and chymotrypsin Acinetobacter calcoaceticus ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 107000, Acinetobacter calcoaceticus, SDS-PAGE Escherichia coli
monomer 1 * 107000, Acinetobacter calcoaceticus, SDS-PAGE Acinetobacter calcoaceticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Escherichia coli
45
-
-
 Acinetobacter calcoaceticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8 7.2 insulin Acinetobacter calcoaceticus