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B6db activities:
Description Glutamate racemase
Catalyzed reaction L-glutamate = D-glutamate
Cofactor Pyridoxal phosphate or no cofactor
Comments 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.

Organisms -Eubacteria
Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Liechti G, Singh R, Rossi PL, Gray MD, Adams NE, Maurelli AT. (2018) Chlamydia trachomatis dapF Encodes a Bifunctional Enzyme Capable of Both d-Glutamate Racemase and Diaminopimelate Epimerase Activities MBio. 9 e00204-18.

 Ferla MP, Brewster JL, Hall KR, Evans GB, Patrick WM. (2017) Primordial-like enzymes from bacteria with reduced genomes. Molecular Microbiology. 105 508-524.

Articles on
last changed 2019/01/29 13:01

B6db activities