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Literature summary for 3.4.23.22 extracted from

  • Williams, D.C.; Whitaker, J.R.; Caldwell, P.V.
    Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease (1972), Arch. Biochem. Biophys., 149, 52-61.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Cryphonectria parasitica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Oxidized B-chain of insulin + H2O the Phe24-Phe25 bond is hydrolyzed at a maximal rate followed by hydrolysis of the Tyr16-Leu17 and Gln4-His5 bonds. The Leu11-Val12 and Asn3-Gln4 bonds are hydrolyzed at slower rates. The Leu11-Val12 bond appears to be considerably more resistant to hydrolysis in the peptide 5-16 than in the intact oxidized B-chain. The Leu15-Tyr16 bond is very slowly hydrolyzed in the peptide 5-16, no hydrolysis in the intact oxidized B-chain. Phe25 is slowly hydrolyzed from the peptide 25-30 and the bond involving Gly20-Glu21 is slowly hydrolyzed in peptide 12-24 and/or peptide 17-24 Cryphonectria parasitica ?
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