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Literature summary for 3.4.24.56 extracted from

  • Song, E.S.; Cady, C.; Fried, M.G.; Hersh, L.B.
    Proteolytic fragments of insulysin (IDE) retain substrate binding but lose allosteric regulation (2006), Biochemistry, 45, 15085-15091.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
2'-O-(2,4,6-trinitrophenyl) adenosine triphosphate ATP-derivative TNP-ATP Rattus norvegicus
3'-O-(2,4,6-trinitrophenyl) adenosine triphosphate ATP-derivative TNP-ATP Rattus norvegicus
ATP regulatory cationic binding site, 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, retain the ability to bind ATP, 4fold activation at 4 mM of 56 kDa fragment, poor activation of the 76 kDa enzyme fragment, overview Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
expression of the N-terminally His6-tagged enzyme in Spodopterafrugiperda Sf9 cells using the baculovirus transfection system Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0059
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, 56 kDa detagged fragment of recombinant His6-tagged enzyme Rattus norvegicus
0.0075
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, 76 kDa detagged fragment of recombinant His6-tagged enzyme Rattus norvegicus
0.0254
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, recombinant His6-tagged full-length enzyme Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amyloid beta-peptide 1-40 + H2O Rattus norvegicus
-
?
-
?
beta-endorphin + H2O Rattus norvegicus
-
?
-
?
insulin + H2O Rattus norvegicus
-
?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification treatment of the recombinant N-terminally His6-tagged IDE with proteinase K leads to the initial cleavage of the His tag and linker region, followed by C-terminal cleavages resulting in intermediate fragments of 95 and 76 kDa and finally a relatively stable 56 kDa fragment, overview Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activities of recombinant His-tagged full-length enzyme and detagged recombinant enzyme fragments with different substrates, overview Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-GGFLRKHGQ-EDDnp + H2O synthetic fluorogenic substrate Rattus norvegicus Abz-GGFLR + KHGQ-EDDnp
-
?
amyloid beta-peptide 1-40 + H2O
-
Rattus norvegicus ?
-
?
amyloid beta-peptide 1-40 + H2O 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP Rattus norvegicus ?
-
?
beta-endorphin + H2O
-
Rattus norvegicus ?
-
?
beta-endorphin + H2O 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP Rattus norvegicus ?
-
?
insulin + H2O
-
Rattus norvegicus ?
-
?
insulin + H2O 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
IDE
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assya at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.72
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, 56 kDa detagged fragment of recombinant His6-tagged enzyme Rattus norvegicus
0.77
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, 76 kDa detagged fragment of recombinant His6-tagged enzyme Rattus norvegicus
93.17
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, recombinant His6-tagged full-length enzyme Rattus norvegicus
104
-
Abz-GGFLRKHGQEDDnp pH 7.4, 37°C, recombinant His6-tagged full-length enzyme Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Rattus norvegicus