EC Number   |
General Information |
Reference |
|---|
   1.14.14.21 | evolution |
DszC with specificity for FMN makes a unique member of the flavin monooxygenase family |
-, 737210 |
| 1.14.14.21 | evolution |
sequence analysis indicates that DszC is similar to the C2 component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH2 and FMNH2 as substrates. The monooxygenase components might be divided into three subclasses: the strictly FMNH2-utilizing subclass, the strictly FADH2-utilizing subclass, and the FMNH2 and FADH2 both-utilizing subclass. DszC has the acyl-CoA dehydrogenase folding and experimentally proves to be able to use both FMNH2 and FADH2 as the substrate, therefore, DszC belongs to the FMNH2 and FADH2 both utilizing subclass, phylogenetic analysis of monooxygenase components of the two-component flavin-dependent monooxygenases |
-, 735785 |
| 1.14.14.21 | malfunction |
site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity |
-, 737210 |
| 1.14.14.21 | metabolism |
DBT monooxygenase from Rhodococcus erythropolis is involved in the first step of the 4S pathway. Dibenzothiophene and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway |
737211 |
| 1.14.14.21 | metabolism |
dibenzothiophene is converted to 2'-hydroxybiphenyl-2-sulfinate by ec1.14.14.21 and 1.14.14.22 in strain F.5.25.8, and the 2'-hydroxybiphenyl-2-sulfinate concentration does not decrease during the stationary phase. Although the production of 2'-hydroxybiphenyl-2-sulfinate appears to proceed in parallel with the increase in biomass, the relationship between the decrease in dibenzothiophene and increase in 2'-hydroxybiphenyl-2-sulfinate does not seem stoichiometric due to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate |
-, 735527 |
| 1.14.14.21 | metabolism |
dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene |
-, 735827 |
| 1.14.14.21 | metabolism |
strain IGTS8 has the ability to convert dibenzothiophene to 2-hydroxybiphenyl with the release of inorganic sulfur. The conversion of dibenzothiophene to 2-hydroxybiphenyl is catalyzed by a multienzyme pathway consisting of two monooxygenases and a desulfinase. The final reaction catalyzed by the desulfinase DszB appears to be the rate limiting step in the pathway |
-, 736855 |
| 1.14.14.21 | metabolism |
the DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species |
-, 736092 |
| 1.14.14.21 | metabolism |
the dibenzothiophene (DBT) desulfurization enzyme system consists of three enzymes: DBT monooxygenase, DBT sulfone monooxygenase, and 2'-hydroxybiphenyl 2-sulfinate desulfinase |
-, 735792 |
| 1.14.14.21 | metabolism |
the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1 |
-, 392304 |
