EC Number   |
Reaction |
Reference |
|---|
    5.1.1.7 | LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate |
molecular dynamics simulations show that the configuration of the distal carbon C6 of L,L-DAP is critical for complex formation since both amino and carboxylate groups are involved in Hbonding interactions with the active site residues. Furthermore, the interactions occurring between the functional groups bonded to the C2 and some residues of the binding cavity immobilize the ligand in a position appropriate for the epimerization reaction, i.e., exactly in the middle of the two catalytic residues Cys73 and Cys217 as confirmed by DFT (density-functional theory) quantum mechanical computation of the Michaelis complex |
675487 |
| 5.1.1.7 | LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate |
molecular mechanism of the enzyme, reversible disulfide bond formation at the active site of CgDapF and disulfide bond-mediated conformational change in CgDapF, domain movement in CgDapF, CgDapF is regulated by redox-switch modulation, via reversible disulfide bond formation, overview |
-, 749346 |
| 5.1.1.7 | LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate |
two-base mechanism for proton translocation. One, but not both, of the proton acceptor sites is a thiol |
- |
