Literature summary for 5.1.1.3 extracted from

Li, Y.; Mortuza, R.; Milligan, D.L.; Tran, S.L.; Strych, U.; Cook, G.M.; Krause, K.L.
Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis (2014), J. Bacteriol., 196, 4239-4244 .

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Application

Application	Comment	Organism
drug development	enzyme MurI is essential and can serve as a target for structure-aided drug design	Mycolicibacterium smegmatis

Cloned(Commentary)

Cloned (Comment)	Organism
gene murI, the murI gene lies in an operon and overlaps MSMEG_4904 at its 5' end by 4 bp. It is closely followed by MSMEG_4902 at its 3' end	Mycolicibacterium smegmatis

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a DELTAmurI strain of Mycobacterium smegmatis, the deletion of the murI gene can be achieved only in minimal medium supplemented with D-glutamate. Gene murI deletion via the gene replacement vector, pKKYL02, temperature-sensitive vector propagation and allelic exchange mutagenesis. Phenotype of DELTAmurI mutant strains on solid minimal medium, DELTAmurI mutant cells display a morphology different from the wild-type cells with pear-shaped swellings at their polar ends, overview	Mycolicibacterium smegmatis

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	A0R1X0	-	-
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155	A0R1X0	-	-

General Information

General Information	Comment	Organism
physiological function	MurI is essential for growth, and glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in Mycobacterium smegmatis	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)