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

BRENDA support

Literature summary for 5.1.1.3 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
Search for more literature for 5.1.1.3

Application

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

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q6L876
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glutamate racemase
-
 Bacillus subtilis
RACE
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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
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]

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

IC50 Value

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

General Information

General Information Comment Organism
physiological function peptidoglycan biosynthesis Bacillus subtilis