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Literature summary for 1.13.11.91 extracted from
- Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis (2016), Arch. Biochem. Biophys., 604, 86-94 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Azotobacter vinelandii | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-mercaptopropanoate + O2 | - |
Azotobacter vinelandii | 3-sulfinopropanoate | - |
? |  |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the pL-dependent activity of MDO can be rationalized assuming a diprotic enzyme model in which three ionic forms of the enzyme are present [cationic, E(z+1), neutral, Ez, and anionic, E(z-1)]. The activities observed for substrates 3-mercaptopropanoate and cysteine appear to be dominated by electrostatic interactions within the enzymatic active site | Azotobacter vinelandii |
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Release 2023.1 (January 2023)
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