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Literature summary for 3.13.2.1 extracted from
- A coupled photometric assay for characterization of S-adenosyl-L-homocysteine hydrolases in the physiological hydrolytic direction (2017), New Biotechnol., 39, 11-17 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Bradyrhizobium elkanii |
| expression in Escherichia coli BL21 (DE3) cells | Bradyrhizobium elkanii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.041 | - |
S-adenosyl-L-homocysteine | 23°C, pH 7.0 | Bradyrhizobium elkanii |  |
| 0.041 | - |
S-adenosyl-L-homocysteine | at pH 8.0 and 25°C | Bradyrhizobium elkanii | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-homocysteine + adenosine | Bradyrhizobium elkanii | - |
S-adenosyl-L-homocysteine + H2O | - |
r | |
| S-adenosyl-L-homocysteine + H2O | Bradyrhizobium elkanii | - |
L-homocysteine + adenosine | - |
? | |
| S-adenosyl-L-homocysteine + H2O | Bradyrhizobium elkanii | - |
L-homocysteine + adenosine | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bradyrhizobium elkanii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bradyrhizobium elkanii |
| Ni-NTA column chromatography | Bradyrhizobium elkanii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-homocysteine + adenosine | - |
Bradyrhizobium elkanii | S-adenosyl-L-homocysteine + H2O | - |
r | |
| S-adenosyl-L-homocysteine + H2O | - |
Bradyrhizobium elkanii | L-homocysteine + adenosine | - |
? | |
| S-adenosyl-L-homocysteine + H2O | - |
Bradyrhizobium elkanii | L-homocysteine + adenosine | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 56000, SDS-PAGE | Bradyrhizobium elkanii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| S-adenosyl-L-homocysteine hydrolase | - |
Bradyrhizobium elkanii |
| S-adenosyl-L-homocysteine hydrolases | - |
Bradyrhizobium elkanii |
| SAHase | - |
Bradyrhizobium elkanii |
| SAHases | - |
Bradyrhizobium elkanii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
- |
Bradyrhizobium elkanii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 35 | the enzyme shows more than 50% activity between 20 and 40°C | Bradyrhizobium elkanii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Bradyrhizobium elkanii |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9 | the enzyme retains more than 70% of its activity at pH values between 7.0 and 9.0, with the maximum activity observed for pH 8.0 | Bradyrhizobium elkanii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Bradyrhizobium elkanii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | a coupled photometric assay for characterization of S-adenosyl-L-homocysteine hydrolases in the physiological hydrolytic direction is developed. The assay is a valuable tool for in vitro characterization of SAHases with biotechnological potential, and for monitoring SAHase activity in diagnostics | Bradyrhizobium elkanii |
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Release 2023.1 (January 2023)
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