EC Number   |
Subunits |
Reference |
|---|
   1.14.12.18 | ? |
construction of a three-dimensional model of alpha-subunit of biphenyl dioxygenase (BphA). BphA active site is composed of two domains, the catalytic domain (residues 1-58 and 176-457) and the Rieske domain (residues 59166). The active site pocket, which is lined mostly by hydrophobic residues (Phe227, Trp390, Phe 376, Asp386, Phe382 and Ala234) is located between the core beta-sheet and alpha-helices in the catalytic domain of the alpha-subunit |
704061 |
| 1.14.12.18 | ? |
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit |
-, 705221 |
| 1.14.12.18 | heterohexamer |
alpha3,beta3, 3 * 53000 + 3 * 27300, measurement of molecular weight and Stokes' radius with gel filtration |
-, 285286 |
| 1.14.12.18 | heterohexamer |
alpha3,beta3, 3 * 53600 + 3 * 25200, SDS-PAGE and gel filtration |
285287 |
| 1.14.12.18 | heterotetramer |
BphA1 (iron-sulfur protein large alpha subunit), BphA2 (iron-sulfur protein small beta subunit), BphA3 (ferredoxin) and BphA4 (ferredoxin reductase). |
-, 693284 |
| 1.14.12.18 | heterotrimer |
oxygenase component, MALDI-TOF |
-, 675223 |
| 1.14.12.18 | More |
three-dimensional model of LY402-BphA1, overview |
-, 726051 |
