EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
    5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Acinetobacter baumannii |
meso-Diaminoheptanedioate |
- |
r |
| 5.1.1.7 | more |
ligand binding to a cleft between the two domains of the enzyme is accompanied by domain closure with strictly conserved cysteine residues, Cys99 and Cys254, positioned to perform acid/base catalysis via a carbanion stabilization mechanism on the stereogenic alpha-carbon atom of the amino acid. Stereochemical control in catalysis is achieved by means of a highly symmetric catalytic site that can accommodate both the L and D stereogenic centers of DAP at the proximal site, whereas specific interactions at the distal site require only the L configuration |
Arabidopsis thaliana |
? |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Bacillus subtilis |
meso-Diaminoheptanedioate |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Bacteria |
meso-Diaminoheptanedioate |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Brevibacillus laterosporus |
meso-Diaminoheptanedioate |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Chlamydia trachomatis |
meso-Diaminoheptanedioate |
- |
r |
| 5.1.1.7 | more |
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 |
? |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Chlamydomonas sp. |
meso-Diaminoheptanedioate |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Corynebacterium glutamicum |
meso-Diaminoheptanedioate |
- |
? |
| 5.1.1.7 | LL-2,6-Diaminoheptanedioate |
- |
Corynebacterium glutamicum |
meso-Diaminoheptanedioate |
- |
r |
