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Results 1 - 10 of 11 > >>
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues - -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues catalytic mechanism, Asp160, Met161, Gly201, Arg202, and Phe219 are involved, active site structure, modeling of enzyme-substrate complex 649123
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues catalytic mechanism, high preference towards large hydrophobic amino terminus residues, active site structure, Glu131 is involved in the catalytic mechanism, enzyme-substrate and enzyme-product complex modeling 653836
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues catalytic pathway and reaction mechanism, catalytic residues are Glu131 and Tyr246, Tyr246 is involved in stabilization of the reaction transition state intermediate, also residue Glu151 is involved 664938
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues catalytic reaction mechanism, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5, involvement of a zinc-bound hydroxide as the reaction nucleophile, Tyr246 polarizes the carbonyl carbon and stabilizes the transition state, enzyme-substrate interaction, overview 686663
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues hydrolyses peptide bonds formed by terminal hydrophobic amino acids such as leucine, methionine, and phenylalanine 651038
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues M161 is involved in substrate binding at the active site cleft 652775
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues preference for hydrophobic residues at the ultimate and the penultimate positions, D-amino acids at these positions reduce the activity, activity is not restricted by the length of substrate chains 651836
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues raction mechanism, catalytic residues are Glu131 and Tyr246, residues Arg202 and Asp160 stabilize the reaction intermediate together with Glu131 663481
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.24release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues structure and reaction mechanism -, 665103
Results 1 - 10 of 11 > >>