1.2.1.65	additional information	enzyme SALDH shows poor activity with NADP+	741638	
1.2.1.65	NAD+	-	288315, 288316, 288317, 288318, 288319, 288320, 288321, 691830, 696505, 741793, 762946	
1.2.1.65	NAD+	amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release	743833	
1.2.1.65	NAD+	dependent on	741638