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Results 1 - 9 of 9
EC Number Natural Substrates Commentary (Nat. Sub.)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19alpha-casein + H2O the enzyme hydrolyses Glu(51)-Tyr(52) and Glu(50)-Glu(51) in Glu(49)-Glu(50)-Glu(51)-Tyr(52) of bovine alphs1-casein
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Gelatin + H2O -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19GluV8 + H2O degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19more enzyme suspected to be involved in the outgrowth of spores when the germinating endospore converts into the vegetative cell
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19more specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19more specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp, key role in degrading the cell-bound Staphylococcus surface adhesion molecules of fibronectin-binding proteins and protein A
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19more splits specifically the peptide bonds formed by alpha-carboxyl groups of glutamic and, and to a lesser extent, of aspartic acid
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19more the enzyme specifically hydrolyzes peptide bonds formed by alpha-carboxyl groups of Glu and Asp residues. Glu-Xaa bonds are cleaved much more efficiently than Asp-Xaa bonds
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19prothrombin + H2O the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin
Results 1 - 9 of 9