Cloned (Comment) | Organism |
---|---|
gene dapF, sequence comparisons and phylogenetic analysis, Chlamydia trachomatis dapF restores growth in an Escherichia coli D-glutamate auxotroph strain WM335 also lacking endogenaous gene dapF, expression under the control of an arabinose-inducible promoter, the recombinant enzyme is capable of both DAP epimerase and D-glut racemase activities, DapFCT is also capable of racemizing D-Glu to L-Glu | Chlamydia trachomatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
LL-2,6-Diaminoheptanedioate | Chlamydia trachomatis | - |
meso-Diaminoheptanedioate | - |
r | |
additional information | Chlamydia trachomatis | Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase, EC 5.1.1.3, and diaminopimelate epimerase activities. DAP and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the pyridoxal 5'-phosphate cofactor | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlamydia trachomatis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
LL-2,6-Diaminoheptanedioate | - |
Chlamydia trachomatis | meso-Diaminoheptanedioate | - |
r | |
additional information | Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase, EC 5.1.1.3, and diaminopimelate epimerase activities. DAP and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the pyridoxal 5'-phosphate cofactor | Chlamydia trachomatis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DapF | - |
Chlamydia trachomatis |
DapFCT | - |
Chlamydia trachomatis |
General Information | Comment | Organism |
---|---|---|
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 | Chlamydia trachomatis |
additional information | the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview | Chlamydia trachomatis |