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Literature summary for 5.1.1.1 extracted from
- Alanine racemase from Tolypocladium inflatum: a key PLP-dependent enzyme in cyclosporin biosynthesis and a model of catalytic promiscuity (2013), Arch. Biochem. Biophys., 529, 55-65.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DTT | optimal activation at 40 mM | Tolypocladium inflatum |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of soluble His-tagged NusA fusion enzyme in Escherichia coli strain HMS174(lambdaDE3) | Tolypocladium inflatum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.4 | - |
D-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
| 4.8 | - |
L-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-alanine | Tolypocladium inflatum | - |
D-alanine | - |
r | |
| additional information | Tolypocladium inflatum | Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions, kinetic analysis and reaction mechanisms, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Tolypocladium inflatum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged NusA fusion enzyme from Escherichia coli strain HMS174(lambdaDE3) by nickel affinity chromatography, ultrafiltration, cleavage of the fusion protein, and anion exchange chromatography | Tolypocladium inflatum |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| L-alanine = D-alanine | reaction mechanism, overview | Tolypocladium inflatum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-alanine | - |
Tolypocladium inflatum | L-alanine | - |
r | |
| L-alanine | - |
Tolypocladium inflatum | D-alanine | - |
r | |
| L-alanine | reversible reaction from an external aldimine in both directions via a quinonoid intermediate, overview | Tolypocladium inflatum | D-alanine | - |
r | |
| additional information | Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions, kinetic analysis and reaction mechanisms, overview | Tolypocladium inflatum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional structure modeling of Tolypocladium inflatum alanine racemase based on the threonine aldolase crystal structure, homology modeling, overview | Tolypocladium inflatum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| tAlaRac | - |
Tolypocladium inflatum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Tolypocladium inflatum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.06 | - |
D-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
| 0.9 | - |
L-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Tolypocladium inflatum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Tolypocladium inflatum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme shows evolutionary and structural similarity to the promiscuous enzymes serine hydroxymethyltransferase, EC 2.1.2.1, and threonine aldolase, EC 4.1.2.48. The three enzymes represent a model of divergent evolution from an ancestral enzyme that was able to catalyse all the reactions of the modern enzymes. Similarly to serine hydroxymethyltransferase and threonine aldolase, Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions | Tolypocladium inflatum |
| physiological function | the pyridoxal 5'-phosphate-dependent enzyme alanine racemase produces the D-alanine incorporated in the cyclic peptide cyclosporine A synthesized by the fungus | Tolypocladium inflatum |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.038 | - |
L-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
| 0.045 | - |
D-alanine | pH 7.6, 37°C, recombinant enzyme | Tolypocladium inflatum | |
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