EC Number   |
Reference |
|---|
   3.4.17.18 | - |
647268 |
| 3.4.17.18 | carboxypeptidase T complexes with substrate analogs benzylsuccinic acid and (2-guanidinoethylmercapto)succinic acid by molecular replacement at resolutions of 1.57 A and 1.62 A. The conservative Leu211 and Leu254 residues are structural determinants for recognition of hydrophobic substrates, whereas Asp263 is for recognition of positively charged substrates. The Pro248-Asp258 loop interacting with Leu254 and Tyr255 is responsible for recognition of the substrate's C-terminal residue. Substrate binding at the S10 subsite leads to the ligand-dependent shift of this loop, and Leu254 side chain movement induces the conformation rearrangement of the Glu277 residue crucial for catalysis |
731804 |
| 3.4.17.18 | crystals of carboxypeptidase T complexes with the transition-state analogs N-sulfamoyl-L-arginine and N-sulfamoyl-L-phenylalanine are grown in microgravity in a capillary using the counter-diffusion technique. Conformation of the transition state analogue of the hydrophobic substrate in the complex with carboxypeptidase T is similar to that of the ground state analogue |
754200 |
| 3.4.17.18 | crystals of the mutant enzyme A243G complexed with N-sulfamoyl-L-phenylalanine are formed under the microgravity conditions by the method of counterx02diffusion through a gel layer in a capillary. The structure of the complex of the CPT G215S/A251G/T257A/D260G/T262D mutant with the transition state analogue N-sulfamoyl-L-phenylalanine is solved at a resolution of 1.35 A and compared it with the structure of similar complex formed by carboxypeptidase T |
752741 |
| 3.4.17.18 | in complex with N-benzyloxycarbonyl-L-leucine, at 1.38 A resolution. The structure of the complex is almost identical to that of the free carboxypeptidase T molecule, and a SO42- ion is also localized in the active site. The S1 subsite of carboxypeptidase T is a very conservative structure and negligibly differs from corresponding sites of carboxypeptidase A and carboxypeptidase B in the composition and the 3D structure. The S1 subsite is close to the catalytic zinc ion and to the residues Arg71, Arg147, Arg129, and Glu277 important for catalysis |
731283 |
| 3.4.17.18 | mutant enzyme G215S/A251G/T257A/D260G/T262D is crystallized and its three-dimensional structure is determined at 1.29 A resolution by X-ray crystallography. The S1' subsite of carboxypeptidase T has not been distorted by the mutagenesis and adequately reproduces the structure of the CPB S1' subsite |
752404 |
| 3.4.17.18 | X-ray diffraction at 2.35 A resolution |
668821 |
