3chu: Difference between revisions

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</table>

== Function ==

[https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:~~20798054~~, PubMed:~~18458342~~). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref>

[https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:18458342, PubMed:20798054). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Line 15:

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chu_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>

<text>to colour the structure by Evolutionary Conservation</text>

</jmolCheckbox>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3chu ConSurf].

== Publication Abstract from PubMed ==

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.

In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.,Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H Proc Natl Acad Sci U S A. 2008 May 13;105(19):6858-63. Epub 2008 May 5. PMID:18458342<ref>PMID:18458342</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

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@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:20798054, PubMed:18458342). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref>
+[https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:18458342, PubMed:20798054). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chu_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3chu ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.,Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H Proc Natl Acad Sci U S A. 2008 May 13;105(19):6858-63. Epub 2008 May 5. PMID:18458342<ref>PMID:18458342</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3chu" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>