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A New Class of Arylamine Oxygenases: Evidence that p ‐Aminobenzoate N‐ Oxygenase (AurF) is a Di‐iron Enzyme and Further Mechanistic Studies
Author(s) -
Simurdiak Michael,
Lee Jungkul,
Zhao Huimin
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600136
Subject(s) - oxygenase , chemistry , enzyme , stereochemistry , class (philosophy) , heme oxygenase , biochemistry , philosophy , heme , epistemology
Alternative route . The p ‐aminobenzoate N‐ oxygenase (AurF) from the aureothin biosynthetic pathway in Streptomyces thioluteus is a novel di‐iron enzyme. Rather than through the previously proposed mechanism, AurF in fact catalyzes the conversion of substrate p ‐aminobenzoate to p ‐nitrobenzoate through at least three consecutive reactions: two monooxygenation steps (a and c) and one dehydrogenation step (b).