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Literature summary extracted from
- Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase (1999), Biochemistry, 38, 3293-3301.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.1.1.1 | hanging drop method, the structure of the enzyme with the inhibitor propionate bound in the active site is determined by X-ray crystallography to a resolution of 1.9 A | Geobacillus stearothermophilus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | acetate | - |
Geobacillus stearothermophilus |  |
| 5.1.1.1 | propionate | - |
Geobacillus stearothermophilus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.1 | Geobacillus stearothermophilus | P10724 | - |
- |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.1.1 | dimer | - |
Geobacillus stearothermophilus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | pyridoxal 5'-phosphate | both active sites of the dimer contain a pyridoxal 5'-phosphate molecule in aldimine linkage to Lys39 as a protonated Schiff base. The protonated pyridoxal 5'-phosphate-Lys39 Schiff base is the reactive form of the enzyme | Geobacillus stearothermophilus | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.1 | 20 | - |
propionate | - |
Geobacillus stearothermophilus | |
| 5.1.1.1 | 92 | - |
acetate | - |
Geobacillus stearothermophilus | |
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Release 2023.1 (January 2023)
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