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Literature summary for 1.7.2.4 extracted from

  • Dreusch, A.; Riester, J.; Kroneck, P.M.; Zumft, W.G.
    Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity. Evidence for disulfide bridges and a putative protein disulfide isomerase gene (1996), Eur. J. Biochem., 237, 447-453.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C165G retaines catalytic activity Pseudomonas stutzeri
C165G Cys165 is not available for Cu cooordination Pseudomonas stutzeri

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm soluble Pseudomonas stutzeri
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu
-
Pseudomonas stutzeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrous oxide + reduced acceptor Pseudomonas stutzeri
-
nitrogen + H2O + acceptor
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas stutzeri
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrous oxide + reduced acceptor
-
Pseudomonas stutzeri nitrogen + H2O + acceptor
-
?