EC Number |
Cofactor |
Reference |
---|
1.2.1.44 | CoA |
- |
673861, 676522 |
1.2.1.44 | NADP+ |
- |
288230, 288231, 288232, 288233, 724494, 725147, 725759, 742589, 743007, 743447 |
1.2.1.44 | NADP+ |
binding structure analysis. Structural comparisons of the NADP+-complexed form of Ph-CCR1 with the apo forms of both Ph-CCR1 and Medicago trunculata Mt-CCR2 reveals a number of adjustments that are localized to polypeptide chain segments surrounding the central cleft and are undoubtedly a direct consequence of NADP+ binding |
743447 |
1.2.1.44 | NADP+ |
not: NADH |
288228, 288234, 389601 |
1.2.1.44 | NADPH |
- |
672472, 673861, 675132, 676451, 676522, 676643, 676843, 712994, 724494, 725147, 725148, 725626, 725759, 726367, 742589, 743007, 743012, 743156, 743233, 743447, 743470, 743848, 762841, 763103, 763522, 763586, 763599, 763691, 763766 |
1.2.1.44 | NADPH |
dependent on |
743501 |
1.2.1.44 | NADPH |
the conserved motifs G-X-X-G-X-X-A and D-X-X-D are reported to be involved in NAD(P) binding and adenine binding pocket stabilization. In addition, the NADP specificity motif R(X)5K is identified, which is a key structure that distinguishes CCR from other NAD(H)-dependent SDRs |
743559 |
1.2.1.44 | NADPH |
the enzyme contains a conserved NAD(P) binding domain VTGAGGFIASWMVKLLLEKGY |
743161 |