Literature summary for 1.7.5.1 extracted from

Vergnes, A.; Pommier, J.; Toci, R.; Blasco, F.; Giordano, G.; Magalon, A.
NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly (2006), J. Biol. Chem., 281, 2170-2176.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	the enzyme-specific chaperone NarJ controls the quality of the enzyme addressed to the membrane via binding to the N-terminal tail of the iron-sulfur containing subunit NarG	Escherichia coli	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mo	the enzyme contains a molybdenum cofactor. The enzyme-specific chaperone NarJ coordinates assembly and molybdenum cofactor acquisition of the heterotrimeric enzyme during the biogenesis process	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrate + reduced methyl viologen	-	Escherichia coli	nitrite + oxidized methyl viologen + H2O	-	?

Synonyms

Synonyms	Comment	Organism
NarGHI	-	Escherichia coli
nitrate reductase A	-	Escherichia coli

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Release 2023.1 (January 2023)