Table 2.
Main functional and structural properties of human D-amino acid oxidase.
| ENZYME PROPERTIES | |||
| Length | 347 residues | ||
| MW (monomer) | 39,474 Da (apoprotein) 40,260 Da (holoenzyme) | ||
| Quaternary structure1 | Dimeric (both holo- and apoprotein) | ||
| FAD affinity1 | 8.0 ± 0.2 μM (free enzyme) 3 ± 1 μM (in complex with benzoate) | ||
| Tm2 | 50.2°C (Apoprotein) 51.8°C (Holoenzyme) 55.7°C (Holoenzyme + CF3-D-Ala) | ||
| KINETIC CONSTANTS1 | |||
| D-Ser | D-Ala | ||
| kcat (s−1) | 6.3 ± 1.4 | 14.7 ± 0.7 | |
| kred (s−1) | 117 ± 6 | 180 ± 20 | |
| APPARENT KINETIC PARAMETERS | |||
| Substrate | kcat (s−1) | Km (mM) | kcat / Km (s−1 mM) |
| D-DOPA3 | 21.7 | 1.5 | 14.5 |
| D-Tyr3 | 14.8 | 1.1 | 13.4 |
| D-Ser | 3.01 | 7.51 | 0.41 |
| 4.03 | 3.93 | 1.03 | |
| D-Phe3 | 15.5 | 1.2 | 12.9 |
| D-Pro1 | 10.2 | 8.5 | 1.2 |
| D-Ala1 | 5.2 | 1.3 | 4.0 |
| D-Asp1 | ~6.7 | ~2,000 | <0.01 |
| Gly1 | 0.9 | 180 | <0.01 |