EC Number   |
General Information |
Reference |
|---|
   3.4.24.19 | evolution |
the enzyme belongs to the astacin family |
733481 |
| 3.4.24.19 | evolution |
the enzyme encoded by bmp1 belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.19 | evolution |
the enzyme encoded by bmp1 belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.19 | evolution |
the enzyme encoded by tld belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.19 | malfunction |
angiogenesis is inhibited by blocking the activity of procollagen C-endopeptidase |
713197 |
| 3.4.24.19 | malfunction |
Inhibition of the enzyme is expected to disrupt fibril formation and stability, preventing the excess collagen deposition associated with fibrosis |
733481 |
| 3.4.24.19 | metabolism |
the N-propeptides are removed first, most probably in the Golgi or in the ERGIC (ER-Golgi intermediate compartment). In contrast, the C-propeptides are cleaved in a post-Golgi compartment |
717224 |
| 3.4.24.19 | metabolism |
the N-propeptides are removed first, most probably in the Golgi or in the ERGIC (ERGolgi intermediate compartment). In contrast, the C-propeptides are cleaved in a post-Golgi compartment |
717224 |
| 3.4.24.19 | more |
the hydrogen bonding residue of the enzyme is Glu219, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.19 | more |
the hydrogen bonding residues of the enzyme are Glu232, Ser294, and Tyr290, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview |
753345 |
