EC Number |
Cofactor |
Reference |
---|
1.1.1.282 | 3-acetylpyridine adenine dinucleotide |
67% of the activity with NAD+ |
654384 |
1.1.1.282 | more |
absolute requirement for a nicotinamide nucleotide cofactor for the oxidation of quinate or shikimate, cofactor specificity, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide |
654384 |
1.1.1.282 | more |
CglQSDH is strictly NAD(H)-dependent due to structural features |
727115 |
1.1.1.282 | more |
in the RifI2 structure, the NADP+-specifying motif is replaced with Asp-Pro-Ser-Thr-Ala-Arg (residues 156-161). The side chain of Asp156 binds to the adenine ribose of NAD+, while its negative charge is predicted to repel the additional phosphate of NADP+. RifI2 possesses low apparent binding affinity for NADP+. Analysis of the cofactor-binding sites of the RifI2ΒNAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview |
740100 |
1.1.1.282 | more |
no activity with NADP+ |
740724 |
1.1.1.282 | more |
the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme |
724089 |
1.1.1.282 | NAD(P)+ |
- |
694093 |
1.1.1.282 | NAD+ |
- |
654384, 654912, 656292, 667700, 669328, 724089, 727115, 740724, 740881, 761708, 762145, 762146 |
1.1.1.282 | NAD+ |
dependent on |
739956 |
1.1.1.282 | NAD+ |
NAD+ binding site, bound very tightly, NAD+ is bound to the Rossmann domain in an elongated fashion with the nicotinamide ring in the pro-R conformation, specificity for binding NAD+ over NADP+ |
644537 |