EC Number |
Reaction |
Reference |
---|
3.4.11.24 | release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues |
- |
- |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release 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 |
3.4.11.24 | release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues |
structure and reaction mechanism |
-, 665103 |