Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cryphonectria parasitica | - |
- |
- |
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 | ? | - |
? |