EC Number |
General Information |
Reference |
---|
1.13.11.39 | metabolism |
2,3-dihydroxybiphenyl 1,2-dioxygenase is an extradiol-type dioxygenase involved in third step of biphenyl degradation pathway |
-, 742643 |
1.13.11.39 | metabolism |
BphC is the key enzyme for polychlorobiphenyl transformation |
724640 |
1.13.11.39 | metabolism |
BphC1 plays a role in the upstream and downstream metabolic pathways of biphenyl, overview |
-, 725631 |
1.13.11.39 | metabolism |
BphC2 might play a supplementary role and contribute more to the upstream than to the downstream pathway of biphenyl, overview |
-, 725631 |
1.13.11.39 | metabolism |
BphC3 plays a role in the upstream and downstream metabolic pathways of biphenyl, overview |
-, 725631 |
1.13.11.39 | metabolism |
the 2,3-DHBP dioxygenase is a key enzyme in the polychlorinated biphenyl degradation pathway |
712995 |
1.13.11.39 | metabolism |
tThe HOO radical species is the reactive oxygen species responsible for the attack of 2,3-dihydroxybiphenyl. The first step in proton-coupled electron transfer is the rate-determining step with a potential energy barrier of 17.2 kcal/mol, close to the experimental value of 14.7 kcal/mol. Residue His194 acts as an acid-base catalyst to deprotonate the hydroxyl group of 2,3-dihydroxybiphenyl at an early stage, then stabilizes the negative charge on the dioxygen group, and finally promotes the semialdehyde product formation as a proton donor |
765269 |
1.13.11.39 | more |
analysis of the interaction between BphC_LA-4 and catecholic substrates by homology modeling and molecular docking, model of the BphC_LA-4-catechol complex, overview. BphC_LA-4 presents lower binding affinity towards 4-methylcatechol in comparison with 3-methylcatechol and catechol. A BphC_LA-4 enzyme electrode prepared by SiO2 sol-gel shows good response to all these three catecholic compounds |
-, 724567 |
1.13.11.39 | more |
enzyme homology modeling, overview |
724640 |
1.13.11.39 | more |
enzyme structure homology modeling, overview |
742574 |