Cloned (Comment) | Organism |
---|---|
cloned in Escherichia coli as a fusion protein with a 6xHis tag at the N-terminus | Bacillus anthracis |
Crystallization (Comment) | Organism |
---|---|
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 | Bacillus anthracis |
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 | Bacillus anthracis |
Protein Variants | Comment | Organism |
---|---|---|
V149A | mutant V149A has about a 2fold higher kcat than wild-type RacE2 (67/sec versus 38/sec), and has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM), in the reverse reaction, V149A has a higher kcat than RacE2 (4.9/sec versus 1.6/sec, respectively), and its Km value for D-glutamate is the same as that of RacE2 (0.2 mM) | Bacillus anthracis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid | D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A | Bacillus anthracis | |
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid | D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A | Bacillus anthracis | |
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid | D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | mutant V149A has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM). In the reverse reaction, the Km of V149A for D-glutamate is the same as that of RacE2 (0.2 mM) | Bacillus anthracis | |
0.2 | - |
D-glutamate | - |
Bacillus anthracis | |
0.9 | - |
D-glutamate | - |
Bacillus anthracis | |
3.7 | - |
L-glutamate | - |
Bacillus anthracis | |
8 | - |
L-glutamate | - |
Bacillus anthracis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
protein extract is loaded on a HiTrap affinity column charged with Co2+, the His-tags are not removed as the enzyme activities with and without these tags are not significantly different | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | - |
Bacillus anthracis | D-glutamate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | both enzymes RacE1 and Rac2 are dimers with monomers arranged in a tail-to-tail orientation which is determined by gel filtration | Bacillus anthracis |
Synonyms | Comment | Organism |
---|---|---|
glutamate racemase | - |
Bacillus anthracis |
RacE1 | - |
Bacillus anthracis |
RacE2 | - |
Bacillus anthracis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus anthracis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | mutant V149A has about a 2fold higher kcat than wild-type RacE2 (67/sec versus 38/sec). In the reverse reaction, V149A has a higher kcat than RacE2 (4.9/sec versus 1.6/sec, respectively) | Bacillus anthracis | |
1.6 | - |
D-glutamate | - |
Bacillus anthracis | |
3.9 | - |
D-glutamate | - |
Bacillus anthracis | |
17.7 | - |
L-glutamate | - |
Bacillus anthracis | |
38 | - |
L-glutamate | - |
Bacillus anthracis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.2 | - |
assay at | Bacillus anthracis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0002 | - |
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid | potent competitive inhibitor for RacE2 mutant V149A | Bacillus anthracis | |
0.0002 | - |
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid | potent competitive inhibitor for RacE2 mutant V149A | Bacillus anthracis | |
0.0003 | - |
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid | potent competitive inhibitor for RacE2 mutant V149A | Bacillus anthracis | |
0.0015 | - |
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid | D-glutamate analog, good competitive inhibitor for RacE1 | Bacillus anthracis | |
0.0035 | - |
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid | D-glutamate analog, good competitive inhibitor for RacE1 | Bacillus anthracis | |
0.0046 | - |
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid | D-glutamate analog, good competitive inhibitor for RacE1 | Bacillus anthracis | |
0.064 | - |
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid | D-glutamate analog, only weak inhibitor of RacE2 | Bacillus anthracis | |
0.073 | - |
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid | D-glutamate analog, only weak inhibitor of RacE2 | Bacillus anthracis | |
0.289 | - |
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid | D-glutamate analog, only weak inhibitor of RacE2 | Bacillus anthracis |