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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. BCDA-treated BsMurI has a single cysteine residue, C185, that is the sole site of modification in over 95% of the inactivated protein. BCDA inhibition of MurI is mechanism-based as opposed to arising from nonspecific interaction with suitably configured cysteine thiols
wild type enzyme, at 25 °C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
mutant T76A, at 25 °C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
mutant T76A, at 25°C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
wild type enzyme, at 25°C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
pH 2.0: about 40% of maximal activity of soluble enzyme, about 60% of maximal activity of immobilized enzyme, pH 10.0: about 80% of maximal activity of immobilized enzyme, about 40% of maximal activity of soluble enzyme
molecular dynamics simulations on the enzyme have suggested particular regions that undergo relatively large changes, both in terms of substrate unbinding, as well as equilibrated enzyme-ligand complexes that show movement relative to one another (i.e., enzyme complexes with different types of active site small molecules equilibrated to distinct conformers)
glutamate racemase (GR) catalyzes the cofactor independent stereoinversion of L- to D-glutamate for biosynthesis of bacterial cell walls. Glutamate racemase is a flexible enzyme capable of binding a variety of small molecules both in the active site and at allosteric binding pockets
glutamate racemase catalyzes stereoinversion at the Calpha of glutamate and is a source of D-glutamate in bacteria, an essential component of the peptidoglycan layer of the bacterial cell walls
while V149A BsGR exhibits a 3- and 6fold increase in the value of Km for L- and D-glutamate relative to wild-type BsGR, respectively, the values of kcat are slightly increased relative to the wild-type enzyme
Tyr53 mutated to the L-(7-hydroxycoumarin-4-yl) ethylglycine (7HC) functional group by site-directed mutagenesis provides ligand-associated fluorescent sensitivity to changes in the local environment (and thus serve as an allosteric reporter), without sacrificing particular contacts with ligands. The placement of the 7HC moiety at the surface of the enzyme, mutant GRY53/7HC mutant, remote from any ligand pockets, places it in a microenvironment where dielectric values are significantly larger, which restricts fluorescence changes to largely water polarization effects. The extraordinary sensitivity of the 7HC moiety within GRY53/7HC, and its incorporation into the dynamic region, provides a valuable experimental probe, quickly identifying a more open and solvated form, which is umwanted for high quality complexation. The GRY53/7HC mutant maintains the same KM value as the wild-type enzyme, but exhibits a 40fold decreased kcat
disruption of enzyme gene yrpC, no effect on growth or production of poly-gamma-glutamte. Disruption of enzyme gene glr, cells are only viable when an exogenous gene copy is present on a plasmid. Glr gene product is responsible for supply of D-glutamate both to the synthesis of peptidoglycan and poly-gamma-glutamate
enzyme knockout mutants, gene racE is essential for growth in rich medium but dispensable for growth in minimal medium. YrpC gene is expressed only in minimal medium. Neither gene is required for synthesis of poly-gamma-DL-glutamate. RacE or yrpC mutant cells accumulate signifcant amounts of D- but not L-glutamate. RacE/yrpC double mutant shows severely impaired D-amino acid utilization
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). The expression of both the plasmid pET15b encoding the enzyme and plasmid pEB-JYRS, encoding the non-natural tRNA harboring the L-(7-hydroxycoumarin-4-yl) ethylglycine (7HC) by an orthogonal tRNA/aminoacyl-tRNA synthetase pair and corresponding tRNA synthetase, within strain BL21(DE3) appears to reduce the overall fitness of the strain, as demonstrated by a reduced growth rate in liquid culture
production of D-glutamate from L-glutamate with glutamate racemase and L-glutamate oxidase from Streptomyces sp. X119-6. Both enzymes are highly stabilized by immobilization
Kada, S.; Nanamiya, H.; Kawamura, F.; Horinouchi, S.
Glr, a glutamate racemase, supplies D-glutamate to both peptidoglycan synthesis and poly-gamma-glutamate production in gamma-PGA-producing Bacillus subtilis
Biosynthesis of a novel glutamate racemase containing a site-specific 7-hydroxycoumarin amino acid enzyme-ligand promiscuity revealed at the atomistic level