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Literature summary extracted from
- Characterization of Lactobacillus salivarius alanine racemase short-chain carboxylate-activation and the role of A131 (2015), SpringerPlus, 4, 639 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | additional information | wild-type enzyme ALR is strongly activated by low concentrations (e.g. 1 mM) of short-chain carboxylates, and is inhibited at higher concentrations (e.g. 10 mM), enzyme residue A131 mediates the activation and stabilization of enzyme ALR by short chain carboxylates | Ligilactobacillus salivarius |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.1 | gene alr, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlusTM(DE3)-RIPL | Ligilactobacillus salivarius |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | A131K | site-directed mutagenesis, the mutant shows a 3fold increased activity compared to wild-type | Ligilactobacillus salivarius |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 5.1.1.1 | acetate increases the stability of enzyme ALR, enzyme residue A131 mediates the activation and stabilization of enzyme ALR by short chain carboxylates | Ligilactobacillus salivarius |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | 2-oxoglutarate | - |
Ligilactobacillus salivarius |  |
| 5.1.1.1 | acetate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | aspartate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | Butyrate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | DL-lactate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | additional information | wild-type enzyme ALR is strongly activated by low concentrations (e.g. 1 mM) of short-chain carboxylates, and is inhibited at higher concentrations (e.g. 10 mM). The enzyme mutant ALRA131K is inhibited at all carboxylate concentrations tested (1-40 mM). Both propionate and butyrate strongly inhibit mutant ALRA131K. ALR and ALRA131K are both inhibited by DL-lactate, though wild-type ALR is inhibited to a lesser degree than ALRA131K. In addition, succinate, pyruvate, 2-oxoglutarate, oxaloacetate, and aspartate also more strongly inhibit mutant ALRA131K than wild-type ALR | Ligilactobacillus salivarius | |
| 5.1.1.1 | oxaloacetate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | propionate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | pyruvate | - |
Ligilactobacillus salivarius | |
| 5.1.1.1 | succinate | - |
Ligilactobacillus salivarius | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.1 | L-alanine | Ligilactobacillus salivarius | - |
D-alanine | - |
r | |
| 5.1.1.1 | L-alanine | Ligilactobacillus salivarius UCC 118 | - |
D-alanine | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.1 | Ligilactobacillus salivarius | Q1WV14 | - |
- |
| 5.1.1.1 | Ligilactobacillus salivarius UCC 118 | Q1WV14 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.1 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlusTM(DE3)-RIPL by nickel affinity chromatography, dialysis, and ultrafiltration | Ligilactobacillus salivarius |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 161 | - |
purified recombinant His-tagged wild-type enzyme, pH 7.0, 30°C | Ligilactobacillus salivarius |
| 5.1.1.1 | 438 | - |
purified recombinant His-tagged mutant A131K enzyme, pH 7.0, 30°C | Ligilactobacillus salivarius |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.1 | L-alanine | - |
Ligilactobacillus salivarius | D-alanine | - |
r | |
| 5.1.1.1 | L-alanine | - |
Ligilactobacillus salivarius UCC 118 | D-alanine | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | ? | x * 43000, recombinant His-tagged enzyme, SDS-PAGE | Ligilactobacillus salivarius |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | ALR | - |
Ligilactobacillus salivarius |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 35 | - |
recombinant wild-type enzyme, without acetate | Ligilactobacillus salivarius |
| 5.1.1.1 | 45 | - |
recombinant enzyme mutant A131K, with or without acetate | Ligilactobacillus salivarius |
| 5.1.1.1 | 50 | - |
recombinant wild-type enzyme, in presence of 1 mM acetate | Ligilactobacillus salivarius |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 8 | - |
recombinant wild-type enzyme, with or without acetate | Ligilactobacillus salivarius |
| 5.1.1.1 | 9 | - |
recombinant enzyme mutant A131K, with or without acetate | Ligilactobacillus salivarius |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | pyridoxal 5'-phosphate | - |
Ligilactobacillus salivarius | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | physiological function | alanine racemase (ALR) is responsible for the high D-alanine production in Lactobacillus salivarius | Ligilactobacillus salivarius |
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