Literature summary extracted from

Gjonaj, L.; Pinkse, M.; Fernandez-Fueyo, E.; Hollmann, F.; Hanefeld, U.
Substrate and cofactor binding to nitrile reductase A mass spectrometry based study (2016), Catal. Sci. Technol., 6, 7391-7397 .

No PubMed abstract available

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.7.1.13	Escherichia coli	Q46920	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.7.1.13	7-cyano-7-carbaguanine + 2 NADPH + 2 H+	-	Escherichia coli	7-aminomethyl-7-carbaguanine + 2 NADP+	-	?
1.7.1.13	additional information	during catalysis each active site of the dimeric enzyme binds one substrate molecule. NADPH binds independent of the substrate. The PreQ0 binding pocket of the active site is not involved in the binding of NADPH	Escherichia coli	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.7.1.13	dimer	mass spectroscopy	Escherichia coli

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.7.1.13	NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)