Literature summary for 5.1.1.3 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.

Search for more literature for 5.1.1.3

Cloned(Commentary)

Cloned (Comment)	Organism
cloned in Escherichia coli	Bacillus anthracis

Protein Variants

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

KM Value [mM]

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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	Q81LA8	-	-
Bacillus anthracis	Q81UL8	-	-

Purification (Commentary)

Purification (Comment)	Organism
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
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)

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

Subunits

Subunits	Comment	Organism
monomer	gel filtration	Bacillus anthracis
More	although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties	Bacillus anthracis
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

Synonyms	Comment	Organism
glutamate racemase	-	Bacillus anthracis
RacE1	-	Bacillus anthracis
RacE2	-	Bacillus anthracis

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

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Release 2023.1 (January 2023)