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000033246 0247_ $$2DOI$$a10.1074/jbc.M009667200
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000033246 084__ $$2WoS$$aBiochemistry & Molecular Biology
000033246 1001_ $$0P:(DE-HGF)0$$aYu, T.-W.$$b0
000033246 245__ $$aMutational analysis and reconstituted expression of the biosynthetic genes involved in the formation of 3-amino-5-hydroxybenzoic acid : the starter unit of rifamycin biosynthesis in Amycolatopsis mediterranei S699
000033246 260__ $$aBethesda, Md.$$bSoc.$$c2001
000033246 300__ $$a12546 - 12555
000033246 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000033246 440_0 $$03091$$aJournal of Biological Chemistry$$v276$$x0021-9258$$y16
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000033246 520__ $$aTo investigate a novel branch of the shikimate biosynthesis pathway operating in the formation of 3-amino-5-hydroxybenzoic acid (AHBA), the unique biosynthetic precursor of rifamycin and related ansamycins, a series of target-directed mutations and heterologous gene expressions were investigated in Amycolatopsis mediterranei and Streptomyces coelicolor. The genes involved in AHBA formation were inactivated individually, and the resulting mutants were further examined by incubating the cell-free extracts with known intermediates of the pathway and analyzing for AHBA formation. The rifL, -M, and -N genes were shown to be involved in the step(s) from either phosphoenolpyruvate/d-erythrose 4-phosphate or other precursors to 3,4-dideoxy-4-amino-d-arabino-heptulosonate 7-phosphate. The gene products of the rifH, -G, and -J genes resemble enzymes involved in the shikimate biosynthesis pathway (August, P. R., Tang, L., Yoon, Y. J., Ning, S., Müller, R., Yu, T.-W., Taylor, M., Hoffmann, D., Kim, C.-G., Zhang, X., Hutchinson, C. R., and Floss, H. G. (1998) Chem. Biol. 5, 69-79). Mutants of the rifH and -J genes produced rifamycin B at 1% and 10%, respectively, of the yields of the wild type; inactivation of the rifG gene did not affect rifamycin production significantly. Finally, coexpressing the rifG-N and -J genes in S. coelicolor YU105 under the control of the act promoter led to significant production of AHBA in the fermented cultures, confirming that seven of these genes are indeed necessary and sufficient for AHBA formation. The effects of deletion of individual genes from the heterologous expression cassette on AHBA formation duplicated the effects of the genomic rifG-N and -J mutations on rifamycin production, indicating that all these genes encode proteins with catalytic rather than regulatory functions in AHBA formation for rifamycin biosynthesis by A. mediterranei.
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000033246 588__ $$aDataset connected to Web of Science, Pubmed
000033246 650_2 $$2MeSH$$aActinomycetales: enzymology
000033246 650_2 $$2MeSH$$aActinomycetales: genetics
000033246 650_2 $$2MeSH$$aAmino Acid Sequence
000033246 650_2 $$2MeSH$$aAminobenzoic Acids: metabolism
000033246 650_2 $$2MeSH$$aBase Sequence
000033246 650_2 $$2MeSH$$aDNA Mutational Analysis: methods
000033246 650_2 $$2MeSH$$aDNA Primers
000033246 650_2 $$2MeSH$$aGenes, Bacterial
000033246 650_2 $$2MeSH$$aGenes, Regulator
000033246 650_2 $$2MeSH$$aMolecular Sequence Data
000033246 650_2 $$2MeSH$$aMultigene Family
000033246 650_2 $$2MeSH$$aOpen Reading Frames
000033246 650_2 $$2MeSH$$aPlasmids
000033246 650_2 $$2MeSH$$aPromoter Regions, Genetic
000033246 650_2 $$2MeSH$$aRestriction Mapping
000033246 650_2 $$2MeSH$$aRifabutin: metabolism
000033246 650_2 $$2MeSH$$aRifamycins: biosynthesis
000033246 650_7 $$00$$2NLM Chemicals$$aAminobenzoic Acids
000033246 650_7 $$00$$2NLM Chemicals$$aDNA Primers
000033246 650_7 $$00$$2NLM Chemicals$$aRifamycins
000033246 650_7 $$072559-06-9$$2NLM Chemicals$$aRifabutin
000033246 650_7 $$076045-71-1$$2NLM Chemicals$$a3-amino-5-hydroxybenzoic acid
000033246 650_7 $$2WoSType$$aJ
000033246 7001_ $$0P:(DE-HGF)0$$aMüller, R.$$b1
000033246 7001_ $$0P:(DE-Juel1)VDB1106$$aMüller, M.$$b2$$uFZJ
000033246 7001_ $$0P:(DE-HGF)0$$aFloss, H. G.$$b3
000033246 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M009667200$$gVol. 276, p. 12546 - 12555$$p12546 - 12555$$q276<12546 - 12555$$tThe @journal of biological chemistry$$v276$$x0021-9258$$y2001
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