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Literature summary extracted from
- Biochemical characterization of alanine racemase -a spore protein produced by Bacillus anthracis (2009), BMB Rep., 42, 47-52.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | pharmacology | potential candidate for the development of a recombinant vaccine | Bacillus anthracis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.1 | expressed as recombinant monomeric protein in Escherichia coli | Bacillus anthracis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | D48A | no effect on the enzyme activity | Bacillus anthracis |
| 5.1.1.1 | K41A | completely inactive | Bacillus anthracis |
| 5.1.1.1 | Y270A | impaired enzyme activity | Bacillus anthracis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | hydroxylamine | non-competitive inhibition kinetics | Bacillus anthracis |  |
| 5.1.1.1 | propionate | propionate influences both Km (affinity for substrate) and Vmax (enzyme catalysis) | Bacillus anthracis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.1 | 3 | - |
L-alanine | - |
Bacillus anthracis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 45000 | - |
SDS-PAGE | Bacillus anthracis |
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 | Bacillus anthracis | - |
D-alanine | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.1 | Bacillus anthracis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.1 | - |
Bacillus anthracis |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.1.1.1 | spore | - |
Bacillus anthracis | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 295 | - |
at 37°C | Bacillus anthracis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.1 | L-alanine | - |
Bacillus anthracis | D-alanine | - |
r | |
| 5.1.1.1 | L-leucine | activity is 20% compared with L-alanine, other amino acids are not racemized | Bacillus anthracis | D-leucine | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | monomer | gel filtration | Bacillus anthracis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | alanine racemase | - |
Bacillus anthracis |
| 5.1.1.1 | ALR | - |
Bacillus anthracis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 37 | - |
- |
Bacillus anthracis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 25 | 45 | - |
Bacillus anthracis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 25 | 85 | between 60 and 70°C 50% of the enzyme activity is lost, at 85°C 50% of the protein molecules are denatured, the residual activity is 4% | Bacillus anthracis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.1 | 22 | - |
L-alanine | - |
Bacillus anthracis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 8.5 | - |
- |
Bacillus anthracis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.1 | 7.5 | 9 | - |
Bacillus anthracis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | pyridoxal 5'-phosphate | PLP is inherently bound to the enzyme, removal of PLP inactivates the enzyme, adding PLP restores the activity, addition of 10 microM PLP to native enzyme slightly enhances activity | Bacillus anthracis | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.1 | 0.16 | - |
hydroxylamine | - |
Bacillus anthracis | |
| 5.1.1.1 | 30 | - |
propionate | - |
Bacillus anthracis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | metabolism | plays a role in spore germination and cell wall biosynthesis | Bacillus anthracis |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.1 | 7.33 | - |
L-alanine | - |
Bacillus anthracis | |
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