Canonical glutamate racemases are PLP-indipendent enzymes.
However, researchers discovered that the cystationine beta-lyases isolated from Wolbachia and Thermotoga maritima exhibit a secondary (but metabolically important) glutamate racemase activity.
Other researchers found that diaminopimelate epimerase (DapF, an enzyme which is typically PLP-independent) encoded by Chlamydia trachomatis is capable of carryng out both the epimerization of DAP and the pyridoxal-phosphate-dependent racemization of glutamate.
Since D-glutamate is present in the cell wall of all bacterial species, the studies mentioned above help explain how bacteria that lack a canonical D-glutamate racemase are capable of synthesizing D-Glu-containing peptidoglycan.
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