EC Number   |
General Information |
Reference |
|---|
    5.1.1.7 | evolution |
the enzyme is a member of the pyridoxal 5'-phosphate-independent racemase family of enzymes |
726632, 727975 |
| 5.1.1.7 | metabolism |
diaminopimelate epimerase (DapF) catalyzes the final step in the synthesis of meso-diaminopimelate, an amino acid unique to peptidoglycan, and synthesizes D-glutamate, EC 5.1.1.3 |
748536 |
| 5.1.1.7 | metabolism |
meso-diaminopimelate is a biosynthetic precursor of L-lysine in bacteria |
726632, 727975 |
| 5.1.1.7 | metabolism |
the enzyme is involved in L-lysine biosynthesis, where it converts LL-diaminopimelate (LL-DAP) into DL-DAP. In the succinylase pathway, LL-diaminopimelate is synthesized from THDP by succinylation, transamination, and desuccinylation steps, LL-DAP is converted to DL-DAP by the action of DAP epimerase. In contrast, in the mDAP dehydrogenase pathway, DAP dehydrogenase converts THDP into DL-DAP in one step, DAP decarboxylase subsequently catalyzes the decarboxylation of DL-DAP to form L-lysine |
-, 749346 |
| 5.1.1.7 | more |
C83 and C221 are catalytic residues |
-, 749346 |
| 5.1.1.7 | more |
dimerization of bacterial diaminopimelate epimerase is essential for catalysis, the enzyme exists in an open, active conformation. The active site of the enzyme resides in a cleft between the two domains with each domain contributing one of the cysteine residues important for catalysis |
727975 |
| 5.1.1.7 | more |
the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview |
748536 |
| 5.1.1.7 | physiological function |
(2R,6S)-2,6-diaminopimelic acid, i.e. meso-diaminopimelate, in the pentapeptide of cell wall peptidoglycan provides the attachment site for the inner or outer membrane to peptidoglycan |
726632 |
| 5.1.1.7 | physiological function |
diaminopimelate epimerase is involved in the biosynthesis of meso-DAP and lysine, which are important precursors for the synthesis of peptidoglycan, housekeeping proteins, and virulence factors in bacteria |
727975 |
| 5.1.1.7 | physiological function |
diaminopimelate isomers are not only intermediates of the lysine biosynthesis diaminopimelate pathway but also essential components of bacterial peptidoglycan |
-, 728008 |
