KEGG   ENZYME: 1.14.99.68
Entry
EC 1.14.99.68               Enzyme                                 

Name
4-aminobenzoate N-oxygenase;
aurF (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
Sysname
4-aminobenzoate,acceptor:oxygen oxidoreductase (N-hydroxylating)
Reaction(IUBMB)
4-aminobenzoate + reduced acceptor + 2 O2 = 4-nitrobenzoate + acceptor + 2 H2O [RN:R12675]
Reaction(KEGG)
R12675
Substrate
4-aminobenzoate [CPD:C00568];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
4-nitrobenzoate [CPD:C18625];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
The enzyme, characterized from the bacterium Streptomyces thioluteus, catalyses an early step in the biosynthesis of the antibiotic aureothin. It contains a carboxylate-bridged binuclear non-heme iron cluster. The native electron donor has not been identified, but is likely an iron-sulfur protein. The reaction mechanism involves formation of an extremely stable peroxo intermediate that catalyses three two-electron oxidations via a hydroxylamine and dihydroxylamine intermediates. cf. EC 1.14.99.67, N-[1-(4-aminophenyl)-1,3-dihydroxypropan-2-yl]-2,2-dichloroacetamide N-oxygenase.
History
EC 1.14.99.68 created 2020
Orthology
K24705  4-aminobenzoate N-oxygenase
Genes
SDV: BN159_2343
SGV: B1H19_35585
SALF: SMD44_07508
KFL: Kfla_4135
PLAB: C6361_01940
PLAT: C6W10_19730
Reference
1  [PMID:15038705]
  Authors
He J, Hertweck C.
  Title
Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: involvement of an unprecedented N-oxygenase.
  Journal
J Am Chem Soc 126:3694-5 (2004)
DOI:10.1021/ja039328t
  Sequence
Reference
2  [PMID:16342311]
  Authors
Lee J, Zhao H.
  Title
Mechanistic studies on the conversion of arylamines into arylnitro compounds by aminopyrrolnitrin oxygenase: identification of intermediates and kinetic studies.
  Journal
Angew Chem Int Ed Engl 45:622-5 (2006)
DOI:10.1002/anie.200502903
Reference
3  [PMID:17765264]
  Authors
Zocher G, Winkler R, Hertweck C, Schulz GE.
  Title
Structure and action of the N-oxygenase AurF from Streptomyces thioluteus.
  Journal
J Mol Biol 373:65-74 (2007)
DOI:10.1016/j.jmb.2007.06.014
  Sequence
Reference
4  [PMID:18458342]
  Authors
Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H.
  Title
In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.
  Journal
Proc Natl Acad Sci U S A 105:6858-63 (2008)
DOI:10.1073/pnas.0712073105
  Sequence
Reference
5  [PMID:19731912]
  Authors
Korboukh VK, Li N, Barr EW, Bollinger JM Jr, Krebs C.
  Title
A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus.
  Journal
J Am Chem Soc 131:13608-9 (2009)
DOI:10.1021/ja9064969
Reference
6  [PMID:20798054]
  Authors
Li N, Korboukh VK, Krebs C, Bollinger JM Jr.
  Title
Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus.
  Journal
Proc Natl Acad Sci U S A 107:15722-7 (2010)
DOI:10.1073/pnas.1002785107
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.68
IUBMB Enzyme Nomenclature: 1.14.99.68
ExPASy - ENZYME nomenclature database: 1.14.99.68
BRENDA, the Enzyme Database: 1.14.99.68

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