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Literature summary for 1.13.11.20 extracted from

  • Faponle, A.S.; Seebeck, F.P.; de Visser, S.P.
    Sulfoxide synthase versus cysteine dioxygenase reactivity in a nonheme iron enzyme (2017), J. Am. Chem. Soc., 139, 9259-9270 .
    View publication on PubMed
Search for more literature for 1.13.11.20

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nonheme iron enzyme Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cysteine + O2 Rattus norvegicus
-
 3-sulfinoalanine
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P21816
-
-

Reaction

Reaction Comment Organism Reaction ID
L-cysteine + O2 = 3-sulfinoalanine catalytic mechanism of cysteine dioxygenase compared to the mechanism of sulfoxide synthase EgtB, EC 1.14.99.50, and its function of the active-site Tyr377 residue. In the sulfoxide syntase reaction, the conserved tyrosine residue reacts via proton-coupled electron transfer with the iron(III)-superoxo species and creates an iron(III)-hydroperoxo intermediate, thereby preventing the possible thiolate dioxygenation side reaction, detailed overview Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
 Rattus norvegicus 3-sulfinoalanine
-
 ?

General Information

General Information Comment Organism
evolution structure and catalytic mechanism comparisons of nonheme iron enzymes cysteine dioxygenase with sulfoxide synthase EgtB, EC 1.14.99.50, quantum mechanics/molecular mechanics calculations, overview Rattus norvegicus
additional information the CDO enzyme active site structure comprises residues Tyr58, Arg60, His86, His88, Cys93, His140, and Tyr157, structure model Rattus norvegicus