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Literature summary extracted from

  • Brunetti, L.; Galeazzi, R.; Orena, M.; Bottoni, A.
    Catalytic mechanism of l,l-diaminopimelic acid with diaminopimelate epimerase by molecular docking simulations (2008), J. Mol. Graph. Model., 26, 1082-1090.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.7 Haemophilus influenzae
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-
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Reaction

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 C–6 of L,L-DAP is critical for complex formation since both amino and carboxylate groups are involved in H–bonding interactions with the active site residues. Furthermore, the interactions occurring between the functional groups bonded to the C–2 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.7 LL-2,6-Diaminoheptanedioate
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Haemophilus influenzae meso-Diaminoheptanedioate
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?

Synonyms

EC Number Synonyms Comment Organism
5.1.1.7 DAP-epimerase
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Haemophilus influenzae
5.1.1.7 diaminopimelate epimerase
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Haemophilus influenzae