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Results 1 - 9 of 9
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O - Cryphonectria parasitica Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2 - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22casein + H2O splits 29.0% of the peptide bonds Cryphonectria parasitica ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O i.e. oxidized insulin B chain, cleavage site specificity Cryphonectria parasitica FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22kappa-casein + H2O reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105 Cryphonectria parasitica ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22more clots milk, not: benzyloxycarbonyl-L-Glu-L-Tyr Cryphonectria parasitica ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22more the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions Cryphonectria parasitica ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22Oxidized 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 ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22Pepsin + H2O splits 8.0% of the peptide bonds Cryphonectria parasitica ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.22Rennin + H2O splits 10.2% of the peptide bonds Cryphonectria parasitica ? - ?
Results 1 - 9 of 9