%0 Journal Article %1 Kim.2004b %A Kim, Yong-Hak %A Moody, Joanna D. %A Freeman, James P. %A Brezna, Barbara %A Engesser, Karl-Heinrich %A Cerniglia, Carl E. %D 2004 %J Journal of industrial microbiology & biotechnology %K alr engesser iswa %N 11 %P 507--516 %R 10.1007/s10295-004-0178-x %T Evidence for the existence of PAH-quinone reductase and catechol-O-methyltransferase in Mycobacterium vanbaalenii PYR-1 %V 31 %X Polycyclic aromatic hydrocarbon (PAH) quinone reductase (PQR) and catechol-O-methyltransferase (COMT), from the PAH-degrading Mycobacterium vanbaalenii PYR-1, were demonstrated to be constitutive enzymes located in the soluble fraction of cell extracts. PQR activities for the reduction of 9,10-phenanthrenequinone and 4,5-pyrene- quinone were 1.40+/-0.13 and 0.12+/-0.01 micromol min(-1) mg-protein(-1), respectively. The exogenous catechols alizarin, anthrarobin, 2,3-dihydroxynaphthalene and esculetin inhibited PQR activity. Anthrarobin (100 microM) and esculetin (100 microM) inhibited 4,5-pyrenequinone reduction by 64-92\%. COMT was involved in the O-methylation of 1,2-dihydroxyphenanthrene to form 1-methoxy-2-hydroxyphenanthrene and 1,2-dimethoxyphenanthrene. Both pyrene and 1-hydroxypyrene were metabolized by M. vanbaalenii PYR-1 to form 1-methoxypyrene, 1-methoxy-2-hydroxypyrene, 1-hydroxy-2-methoxypyrene and 1,2-dimethoxypyrene. Among the catechols tested, anthrarobin showed the highest COMT activity (1.06+/-0.04 nmol/30 min(-1) mg-protein(-1)). These results suggest that the PQR and COMT activities of M. vanbaalenii PYR-1 may play an important role in the detoxification of PAH catechols.

@article{Kim.2004b, abstract = {Polycyclic aromatic hydrocarbon (PAH) quinone reductase (PQR) and catechol-O-methyltransferase (COMT), from the PAH-degrading Mycobacterium vanbaalenii PYR-1, were demonstrated to be constitutive enzymes located in the soluble fraction of cell extracts. PQR activities for the reduction of 9,10-phenanthrenequinone and 4,5-pyrene- quinone were 1.40+/-0.13 and 0.12+/-0.01 micromol min(-1) mg-protein(-1), respectively. The exogenous catechols alizarin, anthrarobin, 2,3-dihydroxynaphthalene and esculetin inhibited PQR activity. Anthrarobin (100 microM) and esculetin (100 microM) inhibited 4,5-pyrenequinone reduction by 64-92{\%}. COMT was involved in the O-methylation of 1,2-dihydroxyphenanthrene to form 1-methoxy-2-hydroxyphenanthrene and 1,2-dimethoxyphenanthrene. Both pyrene and 1-hydroxypyrene were metabolized by M. vanbaalenii PYR-1 to form 1-methoxypyrene, 1-methoxy-2-hydroxypyrene, 1-hydroxy-2-methoxypyrene and 1,2-dimethoxypyrene. Among the catechols tested, anthrarobin showed the highest COMT activity (1.06+/-0.04 nmol/30 min(-1) mg-protein(-1)). These results suggest that the PQR and COMT activities of M. vanbaalenii PYR-1 may play an important role in the detoxification of PAH catechols.}, added-at = {2018-09-05T13:52:51.000+0200}, author = {Kim, Yong-Hak and Moody, Joanna D. and Freeman, James P. and Brezna, Barbara and Engesser, Karl-Heinrich and Cerniglia, Carl E.}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/20895553ae10215ee313940079cb7e73f/steffenhelbich}, doi = {10.1007/s10295-004-0178-x}, interhash = {dee61ced09e60264acf93d8a638e2198}, intrahash = {0895553ae10215ee313940079cb7e73f}, issn = {1367-5435}, journal = {Journal of industrial microbiology {\&} biotechnology}, keywords = {alr engesser iswa}, number = 11, pages = {507--516}, timestamp = {2018-09-05T12:03:32.000+0200}, title = {Evidence for the existence of PAH-quinone reductase and catechol-O-methyltransferase in Mycobacterium vanbaalenii PYR-1}, volume = 31, year = 2004 }