EC Number   |
Reaction |
Reference |
|---|
   3.4.24.B16 | proteolytic degradation of proteins |
- |
- |
| 3.4.24.B16 | proteolytic degradation of proteins |
enzyme might be a modified serine protease with a His residue in the active site, specifically involved in degradation of elastin |
653278 |
| 3.4.24.B16 | proteolytic degradation of proteins |
His120 is critical for LasA activity |
-, 651625 |
| 3.4.24.B16 | proteolytic degradation of proteins |
specific for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin, substrates that contain no Gly-Gly peptide bond, such as beta-casein, appear to be resistant to the enzyme |
651880 |
| 3.4.24.B16 | proteolytic degradation of proteins |
substrate carbonyl oxygen displaces Zn2+-bound water molecule 2, thereby enabling direct interaction with Zn2+ to polarize the peptide carbonyl bond, rendering it susceptible to nucleophilic attack by the second Zn2+-bound water molecule, water molecule1. Water molecule 1 is oriented by interactions with the Nepsilon atoms of both His120 and His81, while that with Zn2+ is weakened. Either of these residues is capable of abstracting a proton from water molecule 1, enabling its addition, as hydroxide, to the substrate carbonyl carbon to generate an oxyanion that is stabilized by bidentate co-ordination of Zn2+ and by interaction with the unprotonated His residue. Proton transfer from the histidine general base to the departing amide nitrogen facilitates cleavage of the peptide bond to generate a product complex |
712754 |
