EC Number   |
Subunits |
Reference |
|---|
   1.14.14.20 | ? |
x * 18000, about, sequence calculation |
-, 736171 |
| 1.14.14.20 | ? |
x * 44200, sequence analysis, monooxygenase subunit of the phenol hydroxylase (PheA1). x * 16900, sequence analysis, flavin reductase subunit of the phenol hydroxylase (PheA2) |
691504 |
| 1.14.14.20 | ? |
x * 57000, about, sequence calculation |
-, 736171 |
| 1.14.14.20 | homodimer |
2 * 17800, PheA2, about, sequence calculation |
-, 736132 |
| 1.14.14.20 | homodimer |
2 * 18000, about, recombinant PheA2 protein, SDS-PAGE |
-, 659279 |
| 1.14.14.20 | homodimer |
2 * 20350, sequence analysis, 2 * 22000, SDS-PAGE, 2 * 22550, mass spectrometry |
-, 701875 |
| 1.14.14.20 | homodimer |
2 * 22550, recombinant His6-tagged PheA2, mass spectrometry, 2 * 20350, sequence calculation, 2 * 22000, recombinant His6-tagged PheA2, SDS-PAGE |
-, 701875 |
| 1.14.14.20 | homodimer |
2 * 57000, SDS-PAGE |
-, 736132 |
| 1.14.14.20 | homodimer |
PheA2 is a single domain homodimeric protein with each FAD-containing subunit being organized around a six-stranded beta-sheet and a capping alpha-helix. The tightly bound FAD prosthetic group binds near the dimer interface, and the re face of the FAD isoalloxazine ring is fully exposed to solvent. PheA2 contains a dual binding cleft for NADH and FAD substrate, which alternate during catalysis |
-, 736400 |
| 1.14.14.20 | homotetramer |
4 * 60720, sequence analysis, 4 * 62000, SDS-PAGE, 4 * 62078, mass spectrometry |
-, 701875 |
