2.5.1.44	NAD+	-	288698, 288700, 288701, 288702, 704662	
2.5.1.44	NAD+	absolute requirement	288698	
2.5.1.44	NAD+	cannot be replaced by NADP+, NADPH, NADH	288697	
2.5.1.44	NAD+	NAD+ seems to function as hydride acceptor in the first part of the reaction and subsequently as hydride donor in the second part	288699	
2.5.1.44	NAD+	required in catalytic amounts with a Km-value of 0.0025 mM	288697	
2.5.1.44	NAD+	unique usage of NAD(H) as a prosthetic group. the cofactor is coordinated through hydrogen bonding via residues Ser21, Ile22, Ser230 (phosphate), Asp45, Val66 (adenosine), Ser92,Thr114, Ala161, Asn162, and Pro163 (nicotineamide riboside). The phosphate-binding motif (18GFGSIG23) is located in the loop connecting beta-strand 2 and alpha-helix A of the Rossmann fold. The adenosine part of NAD+ is bound via loop regions located between beta-strand 4, 5, 6 and alpha-helix C, D, E. Nicotineamide-riboside-binding residues are found in loop regions between beta-strand 7 and 8 and alpha-helix F and O	739672	
2.5.1.44	NADH	unique usage of NAD(H) as a prosthetic group. the cofactor is coordinated through hydrogen bonding via residues Ser21, Ile22, Ser230 (phosphate), Asp45, Val66 (adenosine), Ser92,Thr114, Ala161, Asn162, and Pro163 (nicotineamide riboside). The phosphate-binding motif (18GFGSIG23) is located in the loop connecting beta-strand 2 and alpha-helix A of the Rossmann fold. The adenosine part of NAD+ is bound via loop regions located between beta-strand 4, 5, 6 and alpha-helix C, D, E. Nicotineamide-riboside-binding residues are found in loop regions between beta-strand 7 and 8 and alpha-helix F and O	739672	
2.5.1.44	NADP+	68% of the activity with NAD+	288702