Any feedback?
Literature summary for 2.8.1.1 extracted from
- The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families (2000), J. Mol. Biol., 298, 691-704.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in the sulfur-free state the catalytic Cys residue adopts two alternate conformations, catalytic mechanism relies primarily on the main-chain conformation of the 230 to 235 active-site loop and on a surrounding strong positive electrostatic field | Azotobacter vinelandii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thiosulfate + cyanide | Azotobacter vinelandii | - |
sulfite + thiocyanate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Azotobacter vinelandii | P52197 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thiosulfate + cyanide | - |
Azotobacter vinelandii | sulfite + thiocyanate | - |
? | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
