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Results 1 - 4 of 4
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.65more enzyme SALDH shows poor activity with NADP+ 741638
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.65NAD+ - 288315, 288316, 288317, 288318, 288319, 288320, 288321, 691830, 696505, 741793, 762946
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.65NAD+ 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
Display the word mapDisplay the reaction diagram Show all sequences 1.2.1.65NAD+ dependent on 741638
Results 1 - 4 of 4