EC Number |
Cofactor |
Reference |
---|
4.2.1.46 | NAD+ |
- |
5712, 5713, 5720, 5721, 5722, 5726, 649934, 652851 |
4.2.1.46 | NAD+ |
1 mol of bound NAD+ per mol of enzyme |
5714, 5715, 5718, 5719 |
4.2.1.46 | NAD+ |
coenzyme is tightly bound to the protein |
652771 |
4.2.1.46 | NAD+ |
enzyme consists of an N-terminal NAD+ cofactor-binding domain and a C-terminal sugar-nucleotide binding domain |
701859 |
4.2.1.46 | NAD+ |
required as coenzyme, Lys138 does not play a role in the NAD-binding |
652770 |
4.2.1.46 | NAD+ |
role of NAD+ in catalysis |
5715, 5716, 5717 |
4.2.1.46 | NAD+ |
tightly bound |
650028 |
4.2.1.46 | NAD+ |
tightly bound coenzyme |
650136 |
4.2.1.46 | NADH |
45% of the wild-type enzyme contains NADH during steady-state turnover for each variant by adding a large excess of dTDPglucose, 9% of mutant enzyme D135N, 30% of mutant enzyme D135A, 3% of mutant enzyme E136Q and H232N, 2% of mutant enzyme K199M and K199R, 39% of mutant enzyme Y301F, 8% of mutant enzyme C187A and less than 0.5% of mutant enzymes D135N/E136Q, E198Q, N190D, N190A and H232Q |
650072 |
4.2.1.46 | NADH |
purified enzyme contains coenzyme in the reduced form. The bound NADH is oxidized to NAD+ by adding dTDP-4-keto-6-deoxyglucose. When all the coenzyme is in the oxidized form, the dTDP-sugars remove from the enzyme. In the Y160A variant, almost 98% of the coenzyme is tightly bound NADH. Variants K164M, T134V and Y160F contain 62%, 56% and 35% of bound NADH respectively |
650089 |