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Literature summary extracted from

  • Bordo, D.; Deriu, D.; Colnaghi, R.; Carpen, A.; Pagani, S.; Bolognesi, M.
    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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.1.1 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.1 thiosulfate + cyanide Azotobacter vinelandii
-
sulfite + thiocyanate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.1 Azotobacter vinelandii P52197
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.1 thiosulfate + cyanide
-
Azotobacter vinelandii sulfite + thiocyanate
-
?