Table 3.
Comparison of the proposed key amino-acid residues found in the predicted active sites of AtCAD5, PotSAD, BdCAD3, and BdCAD5
| AtCAD position | AtCAD5 | BdCAD5 | PotSAD | BdCAD3 | Notes |
|---|---|---|---|---|---|
| 49 | T | T | S | T | NADP-binding/ H-shuttle |
| 52 | H | H | H | H | NADP-binding |
| 53 | Q | Q | S | I | Substrate-binding |
| 57 | D | H | D | E | H-shuttle |
| 58 | L | L | W | W | Substrate-binding |
| 60 | M | A | F | N | Substrate-binding |
| 70 | E | E | E | E | Zn-binding |
| 95 | C | V | C | Y | Substrate-binding |
| 119 | W | W | L | L | Substrate-binding |
| 192 | V | V | L | L | NADP-binding |
| 211 | S | S | S | S | NADP-binding |
| 212 | S | S | T | S | NADP-binding |
| 213 | S | S | S | S | NADP-binding |
| 216 | K | K | K | K | NADP-binding |
| 276 | V | V | A | A | Substrate-binding |
| 286 | P | P | F | Y | Substrate-binding |
| 289 | M | M | I | I | Substrate-binding |
| 290 | L | L | A | T | Substrate-binding |
| 299 | F | F | G | G | Substrate-binding |
| 300 | I | I | I | V | Substrate-binding |
| Ratio to AtCAD5 | 20/20 | 17/20 | 7/20 | 7/20 |
Residues were selected based on the published structures of AtCAD5 and PotSAD.