EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.7 | Haemophilus influenzae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
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 | Haemophilus influenzae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.7 | LL-2,6-Diaminoheptanedioate | - |
Haemophilus influenzae | meso-Diaminoheptanedioate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.1.7 | DAP-epimerase | - |
Haemophilus influenzae |
5.1.1.7 | diaminopimelate epimerase | - |
Haemophilus influenzae |