EC Number   |
General Information |
Reference |
|---|
   1.14.12.18 | metabolism |
biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls |
710770 |
| 1.14.12.18 | metabolism |
BPDO is one of the most potent biocatalysts of natural origin for the dioxygenation of chlorobiphenyls |
712774 |
| 1.14.12.18 | more |
the alpha-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase directly influences catalytic activities and substrate specificity, three-dimensional model of LY402-BphA1, overview. The number and subposition of chlorine substituents influence the polychlorinated biphenyls binding ability of BphA1 significantly. Ser283, Val287, Gly321 and Tyr384 residues in the active site of LY402-BphA1 show high variability, and the space limitation of the active site of BphA1 have negative influence on the polychlorinated biphenyls binding affinity of the enzyme |
-, 726051 |
| 1.14.12.18 | more |
the multicomponent enzyme consists of small and large subunits of the oxygenase component, and ferredoxin and reductase components |
724594 |
| 1.14.12.18 | more |
the multicomponent enzyme consists of small and large subunits of the oxygenase component, and ferredoxin and reductase components forming a redox chain in the overall reaction, overview |
725572 |
| 1.14.12.18 | physiological function |
catalyzes critical steps of the bacterial polychlorinated biphenyl degrading pathway |
703342 |
| 1.14.12.18 | physiological function |
catalyzes critical steps of the bacterial polychlorinated biphenyl degrading pathway. Transgenic plants cotransformed with pGreenbphA + bphE + bphG + pGreen-bphF do not produce the three enzyme components simultaneously. Frequency of viable plants among transformants is low, thus simultaneous expression of all four BPDO genes in transgenic tobacco is hampered by genetic or physiological reasons |
703342 |
