1.7.1.13	7-cyano-7-deazaguanine + 2 NADPH + 2 H+	-	Vibrio cholerae	queuine + 2 NADP+	queuine is 7-aminomethyl-7-deazaguanine	?	378400	
1.7.1.13	7-cyano-7-deazaguanine + 2 NADPH + 2 H+	late step in biosynthesis of the modified tRNA nucleoside queuosine	Bacillus subtilis	queuine + 2 NADP+	-	?	378400	
1.7.1.13	7-cyano-7-deazaguanine + 2 NADPH + 2 H+	late step in biosynthesis of the modified tRNA nucleoside queuosine	Escherichia coli	queuine + 2 NADP+	-	?	378400	
1.7.1.13	7-cyano-7-deazaguanine + 2 NADPH + 2 H+	-	Vibrio cholerae ATCC 39315	queuine + 2 NADP+	queuine is 7-aminomethyl-7-deazaguanine	?	378400	
1.7.1.13	7-cyano-7-deazaguanine + 2 NADPH + 2 H+	i.e. preQ0	Escherichia coli	7-aminomethyl-7-deazaguanine + 2 NADP+	-	?	461499	
1.7.1.13	7-cyano-7-deazaguanine + NADPH + H+	-	Escherichia coli	queuine + NADP+ + H+	-	?	425836	
1.7.1.13	additional information	no substrates: acetonitrile, benzonitrile and benzylcyanide	Escherichia coli	?	-	?	89	
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	?	-	?	89	
1.7.1.13	additional information	enzyme is highly specific for substrate preQ0	Pectobacterium carotovorum subsp. carotovorum	?	-	?	89	
1.7.1.13	additional information	QueF binds substrate preQ0 in a strongly exothermic process (DeltaH 80.3 kJ/mol) whereby the thioimide adduct is formed with half-of-the-sites reactivity in the homodimeric enzyme. Both steps of preQ0 reduction involve transfer of the 4-pro-R-hydrogen from NADPH. They proceed about 4-7fold more slowly than trapping of the enzyme-bound preQ0 as covalent thioimide and are mainly rate-limiting for the enzyme's kcat	Escherichia coli	?	-	?	89