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Literature summary for 3.5.1.81 extracted from
- Recombinant production and characterization of an N-acyl-D-amino acid amidohydrolase from Streptomyces sp. 64E6 (2013), World J. Microbiol. Biotechnol., 29, 899-906.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | N-acyl-D-amino acid amidohydrolases are often used as tools for the optical resolution of D-amino acids, which are important products with applications in industries related to medicine and cosmetics | Streptomyces sp. |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning by sequence-based screening, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli and Streptomyces lividans | Streptomyces sp. |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates | Streptomyces sp. |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces sp. | S0AUN2 | - |
- |
| Streptomyces sp. 64E6 | S0AUN2 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:glucose-grown cell | when using glycerol as a carbon source for cultivation, the recombinant enzyme from Streptomyces sp. 64E6 is produced in 4.2fold greater quantities by Streptomyces lividans than when using glucose | Streptomyces sp. | - |
| culture condition:glycerol-grown cell | when using glycerol as a carbon source for cultivation, the recombinant enzyme from Streptomyces sp. 64E6 is produced in 4.2fold greater quantities by Streptomyces lividans than when using glucose | Streptomyces sp. | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
0.05-6.32 U/mg, substrate N-acetyl-D-phenylalanine, different lines, pH and temperature not specified in the publication, in absence of Co2+ | Streptomyces sp. |
| 7.34 | - |
substrate N-acetyl-D-phenylalanine, pH and temperature not specified in the publication, in presence of Co2+ | Streptomyces sp. |
| 9.31 | - |
substrate N-acetyl-D-methionine , pH and temperature not specified in the publication, in presence of Co2+ | Streptomyces sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme hydrolyzes various N-acetyl-D-amino acids that have hydrophobic side chains. The activity toward N-chloroacetyl-D-Phe is 2.1-fold higher than that toward N-acetyl-D-Phe, indicating that the structure of N-acylated portion of substrate alters the activity | Streptomyces sp. | ? | - |
? | |
| additional information | the enzyme hydrolyzes various N-acetyl-D-amino acids that have hydrophobic side chains. The activity toward N-chloroacetyl-D-Phe is 2.1-fold higher than that toward N-acetyl-D-Phe, indicating that the structure of N-acylated portion of substrate alters the activity | Streptomyces sp. 64E6 | ? | - |
? | |
| N-acetyl-D-methionine + H2O | - |
Streptomyces sp. | acetate + D-methionine | - |
? | |
| N-acetyl-D-methionine + H2O | - |
Streptomyces sp. 64E6 | acetate + D-methionine | - |
? | |
| N-acetyl-D-phenylalanine + H2O | - |
Streptomyces sp. | acetate + D-phenylalanine | - |
? | |
| N-acetyl-D-phenylalanine + H2O | - |
Streptomyces sp. 64E6 | acetate + D-phenylalanine | - |
? | |
| N-chloroacetyl-D-phenylalanine + H2O | 2.1-fold higher activity compared to N-acetyl-D-Phe | Streptomyces sp. | chloroacetate + D-phenylalanine | - |
? | |
| N-chloroacetyl-D-phenylalanine + H2O | 2.1-fold higher activity compared to N-acetyl-D-Phe | Streptomyces sp. 64E6 | chloroacetate + D-phenylalanine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-Aminoacylase | - |
Streptomyces sp. |
| N-Acyl-D-amino acid amidohydrolase | - |
Streptomyces sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
purifed recombinant enzyme, stable up to | Streptomyces sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | - |
Streptomyces sp. |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 9 | purifed recombinant enzyme, stable at | Streptomyces sp. |
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