5.1.1.3: glutamate racemase
This is an abbreviated version!
For detailed information about glutamate racemase, go to the full flat file.
Word Map on EC 5.1.1.3
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5.1.1.3
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peptidoglycan
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l-glutamate
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cofactor-independent
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drug development
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pediococcus
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poly-gamma-glutamate
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pyrophilus
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pentosaceus
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fermenti
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ciceri
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stereoinversion
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medicine
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synthesis
- 5.1.1.3
- peptidoglycan
- l-glutamate
-
cofactor-independent
- drug development
- pediococcus
-
poly-gamma-glutamate
- pyrophilus
- pentosaceus
- fermenti
-
ciceri
-
stereoinversion
- medicine
- synthesis
Reaction
Synonyms
AAR, BAS0806, BAS4379, BcGR, BsGR, BsRacE, CBL/ALR, cystathionine beta-lyase, D-glutamate racemase, DapF, FnGR, GBAA_0847, GBAA_4717, GLR, GluR, glutamate racemase, glutamic acid racemases, GRL, HpMurI, MetC, More, MurI, RACE, RacE1, RacE2, Racemase, glutamate, Rv1338, TmCBL, wMelCBL
ECTree
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Crystallization
Crystallization on EC 5.1.1.3 - glutamate racemase
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hanging drop vapor diffusion method, crystal structure of apo-enzyme and enzyme complexed with a substrate analog, D-glutamine, by multiwavelength anomalous dispersion method using a thimerosal-bound MurI crystal, determined at 2.3 A resolution
crystallization trials are performed by the hanging-drop, vapor-diffusion method, X-ray structure analysis shows that RacE1 and RacE2 are both dimers with monomers arranged in a tail-to-tail orientation, RCSB Protein Data Bank: 2GZM
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crystallization trials are performed by the hanging-drop, vapor-diffusion method. X-ray structure analysis shows that RacE1 and RacE2 are both dimers with monomers arranged in a tail-to-tail orientation, RCSB Protein Data Bank: 2DWU
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crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
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crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
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crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. The Escherichia coli MurI co-crystallizes as a monomer with both L-glutamate and its activator UDP-MurNAc-Ala. The activator binds in the hinge region on the side opposite to the catalytically active site through contacts between the uracil ring system and domain B and through specific salt bridge interactions with R104 in domain A and the alanyl moiety of the activator, consistent with the strict requirement of the alanine and uracil moieties for activation
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the different kinetic profiles of MurI enzymes across the species suggest fundamental structural differences and therefore, crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. The Helicobacter pylori MurI enzyme also forms a homodimer but with the active sites in close proximity in a face-to-face orientation
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purified recombinant enzyme complexed with D-glutamate, microbatch-underoil method, mixing of 0.002 ml of 5 mg/ml protein in 20 mM Tris HCl, pH 8.0, and 1 mM D-glutamate, with 0.001 ml of crystallizing solution containing 0.1 M HEPES, pH 7.5, and 20% PEG 10000, 18°C, 14 days, X-ray diffraction structure determination and analysis at 2.30 A resolution
purified recombinant enzyme complexed with D-glutamate, hanging drop vapour diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 20 mM Tris HCl, pH 8.0, and 1 mM D-glutamate, with 0.002 ml of 18% PEG3350, 0.2 M NaI, 4°C, 4 days, X-ray diffraction structure determination and analysis at 1.76 A resolution
crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
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crystallization is carried out by the sitting-drop,vapor-diffusion method, crystal structures of GluR from Streptococcus pyogenes in both inhibitor-free and inhibitor-bound forms. The inhibitor-free GluR crystallizes in two different forms, which diffracts to 2.25 A and 2.5 A resolution, while the inhibitor-bound crystal diffracted to 2.5 A resolution.