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Literature summary for 5.1.1.3 extracted from
- Biochemical characterization of glutamate racemase - a new candidate drug target against Burkholderia cenocepacia infections (2016), PLoS ONE, 11, e0167350 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is a good target for antibacterial drug development for treatment of Burkholderia cenocepacia infections causing cystic fibrosis | Burkholderia cenocepacia |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Burkholderia cenocepacia |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (2R)-2-amino-4-benzylpentanedioic acid | - |
Burkholderia cenocepacia |  |
| 1H-benzimidazole-2-sulfonic acid | - |
Burkholderia cenocepacia | |
| 4-hydroxybenzene-1,3-disulfonate | - |
Burkholderia cenocepacia | |
| bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex | binding structure, overview | Burkholderia cenocepacia | |
| Cu2+ | inhibition is completely reversed by EDTA | Burkholderia cenocepacia | |
| dipicolinic acid | - |
Burkholderia cenocepacia | |
| Mn2+ | inhibition is completely reversed by EDTA | Burkholderia cenocepacia | |
| additional information | library screening for inhibitory compounds, two Zn (II) and Mn (III) 1,3,5-triazapentadienate complexes are found to efficiently inhibit the glutamate racemase activity. The metal complexes affect the enzyme activity by binding to the enzyme-substrate complex and promoting the formation of an inhibited dimeric form of the enzyme. Evaluation of a series of compounds, including 1H-benzimidazole-2-sulfonic acid, dipicolinic acid, 4-hydroxybenzene-1,3-disulfonate, and (2R)-2-amino-4-benzylpentanedioic acid, which are already known inhibitors of different bacterial glutamate racemases, for inhibitory activity on the enzyme, inhibition mechanism of BcGR by metal complexes, overview | Burkholderia cenocepacia | |
| tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex | binding structure, overview | Burkholderia cenocepacia | |
| Zn2+ | inhibition is completely reversed by EDTA | Burkholderia cenocepacia | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | recombinant enzyme, steady state kinetic analysis | Burkholderia cenocepacia | |
| 13.89 | - |
D-glutamate | recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no effects on activity by Mg2+, Fe2+, and Ni2+ | Burkholderia cenocepacia |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 31000 | - |
recombinant detagged monomeric enzyme, gel filtration | Burkholderia cenocepacia |
| 70000 | - |
recombinant detagged dimeric enzyme, gel filtration | Burkholderia cenocepacia |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | Burkholderia cenocepacia | - |
D-glutamate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Burkholderia cenocepacia | - |
- |
- |
| no activity in Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage with the PreScission protease, dialysis and another step of nickel affinity chromatography, to homogeneity | Burkholderia cenocepacia |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.4 | - |
purified recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glutamate | - |
Burkholderia cenocepacia | L-glutamate | - |
r | |
| L-glutamate | - |
Burkholderia cenocepacia | D-glutamate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 30000, about, SDS-PAGE | Burkholderia cenocepacia |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BcGR | - |
Burkholderia cenocepacia |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 50 | - |
Burkholderia cenocepacia |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 50 | maximal activity at 40-50°C, 80% activity at 37°C | Burkholderia cenocepacia |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
purified recombinant enzyme, pH 8.0, moderately stable preserving more than 80% of initial activity after 2 h at up to 40°C, but rapidly loses all activity at higher temperatures | Burkholderia cenocepacia |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.025 | - |
D-glutamate | recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | - |
Burkholderia cenocepacia |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | enzyme exhibits a preference for high pH values, showing an optimal activity at pH 8.0-9.0, with about 70% of maximal activity at pH 9.5, and less than 50% activity below pH 7.0 | Burkholderia cenocepacia |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9.5 | purified recombinant enzyme, 37°C, full activity is almost preserved at pH values pH 7.0-8.5, whereas the stability dramatically decreases at pH values below pH 6.0 or up to pH 9.5, with less than 40% of the initial activity remaining | Burkholderia cenocepacia |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Burkholderia cenocepacia | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.01 | - |
recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia | tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex | |
| 0.0353 | - |
recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia | bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex | |
| 0.15 | - |
recombinant enzyme, pH 8.0, 37°C | Burkholderia cenocepacia | dipicolinic acid | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure homology modeling, in BcGR, all critical residues for enzymatic activity and substrate recognition are fully conserved within the 2-domain glutamate racemase fold | Burkholderia cenocepacia |
| physiological function | glutamate racemase is an essential enzyme for the biosynthesis of the bacterial cell wall | Burkholderia cenocepacia |
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