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Literature summary for 1.4.1.1 extracted from
- Heterologous expression and partial characterization of a new alanine dehydrogenase from Amycolatopsis sulphurea (2021), Protein J., 40, 342-347 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme from Amycolatopsis sulphurea has the ability to produce valuable molecules for various industrial purposes and represents a potential biocatalyst for biotechnological applications | Amycolatopsis sulphurea |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene AlaDH, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Amycolatopsis sulphurea |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Amycolatopsis sulphurea | |
| 2.03 | - |
L-alanine | pH 10.5, 25°C, recombinant enzyme | Amycolatopsis sulphurea |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-alanine + H2O + NAD+ | Amycolatopsis sulphurea | - |
pyruvate + NH3 + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Amycolatopsis sulphurea | A0A2A9FGJ5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Amycolatopsis sulphurea |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-alanine + H2O + NAD+ | - |
Amycolatopsis sulphurea | pyruvate + NH3 + NADH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 41090, His6-tagged enzyme, sequence calculation, x * 38930, nontagged enzyme, sequence calculation | Amycolatopsis sulphurea |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ALADH | - |
Amycolatopsis sulphurea |
| AsAlaDH | - |
Amycolatopsis sulphurea |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
oxidative deamination of L-alanine | Amycolatopsis sulphurea |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 60 | purified recombinant AsAlaDH, optimum temperature for oxidative deamination activity is 25°C. Enzyme activity decreases sharply above 50°C | Amycolatopsis sulphurea |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 55 | AlaDH retains about 10% of maximal activity at 55°C and about 90% at 50°C | Amycolatopsis sulphurea |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13.24 | - |
L-alanine | pH 10.5, 25°C, recombinant enzyme | Amycolatopsis sulphurea | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
oxidative deamination of L-alanine | Amycolatopsis sulphurea |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 11 | purified recombinant AsAlaDH lost activity rapidly at pH 11.0 or higher, while retaining more than 50% activity at pH 9.5. It shows less than 10% activity at neutral pH 7.0 and almost no activity at pH 3.0-6.5 | Amycolatopsis sulphurea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Amycolatopsis sulphurea | |
| NADH | - |
Amycolatopsis sulphurea | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Amycolatopsis sulphurea | isoelectric focusing | - |
5.7 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | AlaDH catalyzes the reversible conversion of L-alanine and pyruvate, which has an important role in the TCA energy cycle | Amycolatopsis sulphurea |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 6.52 | - |
L-alanine | pH 10.5, 25°C, recombinant enzyme | Amycolatopsis sulphurea | |
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