In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.

@article{citeulike:2812218, abstract = {p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme activity, the crystal structure of AurF in the oxidized state, and the cocrystal structure of AurF with its product pNBA. Our combined biochemical and structural analysis unequivocally indicates that AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates.}, address = {Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.}, author = {Choi, Y. S. and Zhang, H. and Brunzelle, J. S. and Nair, S. K. and Zhao, H. }, citeulike-article-id = {2812218}, doi = {http://dx.doi.org/10.1073/pnas.0712073105}, issn = {1091-6490}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {enzymatic-oxidation, enzyme, n-oxidation}, month = {May}, number = {19}, pages = {6858--6863}, posted-at = {2008-05-19 09:19:19}, priority = {2}, title = {In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.}, url = {http://dx.doi.org/10.1073/pnas.0712073105}, volume = {105}, year = {2008} }

TY - JOUR ID - citeulike:2812218 L3 - citeulike-article-id:2812218 TI - In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis. JF - Proceedings of the National Academy of Sciences of the United States of America VL - 105 IS - 19 SP - 6858 EP - 6863 AD - Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. SN - 1091-6490 N2 - p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme activity, the crystal structure of AurF in the oxidized state, and the cocrystal structure of AurF with its product pNBA. Our combined biochemical and structural analysis unequivocally indicates that AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates. KW - enzymatic-oxidation KW - enzyme KW - n-oxidation AU - Choi, YS AU - Zhang, H AU - Brunzelle, JS AU - Nair, SK AU - Zhao, H PY - 2008/05/13/ UR - http://dx.doi.org/10.1073/pnas.0712073105 ER -