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Literature summary extracted from

  • Dodd, D.; Reese, J.G.; Louer, C.R.; Ballard, J.D.; Spies, M.A.; Blanke, S.R.
    Functional comparison of the two Bacillus anthracis glutamate racemases (2007), J. Bacteriol., 189, 5265-5275.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.3 cloned in Escherichia coli Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.3 C185A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold Bacillus anthracis
5.1.1.3 C188A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold Bacillus anthracis
5.1.1.3 C74A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold Bacillus anthracis
5.1.1.3 C77A predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold Bacillus anthracis
5.1.1.3 additional information RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 0.77
-
D-glutamate
-
Bacillus anthracis
5.1.1.3 1
-
D-glutamate
-
Bacillus anthracis
5.1.1.3 14
-
L-glutamate
-
Bacillus anthracis
5.1.1.3 38
-
L-glutamate
-
Bacillus anthracis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.3 32320
-
predicted cDNA Bacillus anthracis
5.1.1.3 32530
-
predicted from cDNA Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Bacillus anthracis Q81LA8
-
-
5.1.1.3 Bacillus anthracis Q81UL8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3 RacE1 is expressed as in Escherichia coli with an amino-terminal hexahistidine fusion peptide to facilitate purification via nickel-chelate affinity chromatography Bacillus anthracis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.3 additional information
-
in Bacillus anthracis glutamate racemase is encoded by two genes racE1 and racE2, both enzymes are different in quaternary structure and catalyze the reversible stereoisomerization with similar but not identical kinetic properties Bacillus anthracis

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
5.1.1.3 monomer gel filtration Bacillus anthracis
5.1.1.3 More although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties Bacillus anthracis
5.1.1.3 More by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes Bacillus anthracis

Synonyms

EC Number Synonyms Comment Organism
5.1.1.3 glutamate racemase
-
Bacillus anthracis
5.1.1.3 RacE1
-
Bacillus anthracis
5.1.1.3 RacE2
-
Bacillus anthracis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.3 25
-
assay at Bacillus anthracis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.3 1.8
-
D-glutamate
-
Bacillus anthracis
5.1.1.3 2
-
D-glutamate
-
Bacillus anthracis
5.1.1.3 12
-
L-glutamate
-
Bacillus anthracis
5.1.1.3 18
-
L-glutamate
-
Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.3 8.1
-
maximum activity Bacillus anthracis
5.1.1.3 8.2
-
maximum activity Bacillus anthracis