Earticle

초록

영어

p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthease starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. Homologous AurF proteins are expected to be also involved in the biosynthesis of other aromatic nitro compounds such as spectinabilin, alloaureothin, griseulin and SNF4435C/D. 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 controversy1,2. Here we report the in vitro reconstitution of the enzymatic activity by both biological and chemical methods, the crystal structure of AurF in oxidized state, and the co-crystal structure of AurF with product pNBA. Our combined biochemical and structural analysis unequivocally indicate that AurF is a nonheme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitrosoamine intermediates.

저자

• Yoo Seong Choi [ Department of Chemical and Biomolecular Engineering ]
• Houjin Zhang [ Department of Biochemistry, University Illinois at Urbana-Champaign, Urbana, IL 61801, USA ]
• Joseph S. Brunzelle [ Life Sciences Collaborative Access Team, Argonne National Labs., Argonne, IL 60439, USA ]
• Satish Nair [ Department of Biochemistry, University Illinois at Urbana-Champaign, Urbana, IL 61801, USA ]
• Huimin Zhao [ Department of Chemical and Biomolecular Engineering, University Illinois at Urbana-Champaign, Urbana, IL 61801, USA ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576