Literature summary 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.

Protein Variants

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

Localization

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

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.7.2.4	Cu	-	Pseudomonas stutzeri

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.7.2.4	Pseudomonas stutzeri	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)