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Literature summary for 3.4.24.56 extracted from

  • Baskin, F.K.; Kitachi, A.E.
    Substrate studies for insulin-specific protease (1973), Eur. J. Biochem., 37, 489-496.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000158
-
desalanine-insulin
-
Rattus norvegicus
0.000022
-
Insulin
-
Rattus norvegicus
0.0000244
-
monoarginine-insulin diarginine-insulin Rattus norvegicus
0.000044
-
destridecapeptide-proinsulin
-
Rattus norvegicus
0.000055
-
desnonapeptide-proinsulin
-
Rattus norvegicus
0.000176
-
desdipeptide-proinsulin
-
Rattus norvegicus
0.0002342
-
Proinsulin cleaved Rattus norvegicus
0.0008572
-
Proinsulin
-
Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Rattus norvegicus
-
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
desalanine-insulin + H2O
-
Rattus norvegicus ?
-
?
desdipeptide-proinsulin + H2O
-
Rattus norvegicus ?
-
?
desnonapeptide-proinsulin + H2O
-
Rattus norvegicus ?
-
?
destridecapeptide-proinsulin + H2O
-
Rattus norvegicus ?
-
?
Insulin + H2O
-
Rattus norvegicus Hydrolyzed insulin
-
?
monoarginine-insulin + H2O
-
Rattus norvegicus ?
-
?
additional information requirement for optimal substrate activity is the deblocking of the amino end of the A-chain Rattus norvegicus ?
-
?
Porcine proinsulin intermediates + H2O cleaved proinsulin, desdipeptide-proinsulin, desnonapeptide-proinsulin, destridecapeptide-proinsulin, desalanine-insulin, monoarginine-insulin and diarginine-proinsulin are degraded at 19.8%, 25.6%, 63.5%, 73.7%, 101.5%, 98% and 98% of the activity of insulin, respectively Rattus norvegicus ?
-
?