B6db activities : 5_1_1

	Activities \| Families \| Sequences \| Fold types \| References \| Help


	5.1.1.3
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) 5.1.1.3 BRENDA (activities) 5.1.1.3 KEGG (pathways) 5.1.1.3 PLPMDB (PLP mutants) 5.1.1.3

References	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 5.1.1.3

last changed	2019/01/29 13:01