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Literature summary for 1.7.1.6 extracted from
- Purification, characterization, and crystal structure of YhdA-type azoreductase from Bacillus velezensis (2021), Proteins, 89, 483-492 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | - |
Bacillus velezensis |  |
| dithiothreitol | - |
Bacillus velezensis | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Bacillus velezensis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| using 50 mM monobasic potassium phosphate and 20% polyethylene glycol 8000 | Bacillus velezensis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme is oxygen-insensitive | Bacillus velezensis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 69900 | - |
SEC-MALS | Bacillus velezensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus velezensis | B3VPZ9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA affinity column chromatography | Bacillus velezensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Congo Red + NADPH + H+ | the enzyme decolorizes 9% of 0.04 mM Congo Red in 15 min | Bacillus velezensis | ? | - |
? | |
| Methyl Orange + NADPH + H+ | the enzyme decolorizes more than 14% of 0.04 mM Methyl Orange in 15 min | Bacillus velezensis | ? | - |
? | |
| methyl red + NADH + H+ | the rate of reaction is about 7.14 times faster with NADPH at different concentrations of Methyl Orange as compared to that with NADH | Bacillus velezensis | ? | - |
? | |
| methyl red + NADPH + H+ | the enzyme decolorizes more than 50% of 0.04 mM Methyl Red in 15 min | Bacillus velezensis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 20000, SDS-PAGE | Bacillus velezensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| azoreductase | - |
Bacillus velezensis |
| YhdA | - |
Bacillus velezensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Bacillus velezensis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 60 | at high temperature of 50°C, the enzyme shows about 79% activity of that at 37°C. On further increasing the temperature to 60°C, the activity drops to 64%, while the activity is 80% at low temperature of 20°C | Bacillus velezensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
melting temperature of 89.5°C | Bacillus velezensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | - |
Bacillus velezensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | - |
Bacillus velezensis | |
| NADPH | favored electron donor | Bacillus velezensis | |
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Release 2023.1 (January 2023)
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