Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Spies, M.; Reese, J.; Dodd, D.; Pankow, K.; Blanke, S.; Baudry, J.
    Determinants of catalytic power and ligand binding in glutamate racemase (2009), J. Am. Chem. Soc., 131, 5274-5284.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.1.1.3 drug development glutamate racemase is an attractive target for the design of antibacterial agents Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.3 recombinant wild type and mutant proteins are expressed in Escherichia coli cells Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.3 T76A production by site-directed mutagenesis, strong RacE-glutamate carbanion interaction energy is notably dissipated with the mutant Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.3 3-sulfobenzoic acid structural analogue of dipicolinate dianion Bacillus subtilis
5.1.1.3 dipicolinate dianion DPA Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 0.25
-
 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 Bacillus subtilis
5.1.1.3 8.6
-
 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 Bacillus subtilis
5.1.1.3 14
-
 L-glutamate wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0 at 25°C in the presence of 0.22 microM glutamate racemase Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.3 L-glutamate Bacillus subtilis
-
 D-glutamate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Bacillus subtilis Q6L876
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3 by using nickel-chelate chromatography Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.3 L-glutamate
-
 Bacillus subtilis D-glutamate
-
 r

Synonyms

EC Number Synonyms Comment Organism
5.1.1.3 glutamate racemase
-
 Bacillus subtilis
5.1.1.3 RACE
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.3 0.43
-
 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 Bacillus subtilis
5.1.1.3 1.3
-
 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 Bacillus subtilis
5.1.1.3 87
-
 L-glutamate wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0, at 25°C in the presence of 0.22 microM glutamate racemase Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.1.3 1.97
-
 dipicolinate dianion competitive inhibition Bacillus subtilis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
5.1.1.3 2.9
-
 structural analogue of dipicolinate dianion Bacillus subtilis 3-sulfobenzoic acid

General Information

EC Number General Information Comment Organism
5.1.1.3 physiological function peptidoglycan biosynthesis Bacillus subtilis