Literature summary for 1.7.1.13 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

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q46920	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7-cyano-7-carbaguanine + 2 NADPH + 2 H+	-	Escherichia coli	7-aminomethyl-7-carbaguanine + 2 NADP+	-	?
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

Subunits	Comment	Organism
dimer	mass spectroscopy	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)