Molecular and Catalytic Properties of Monoacetylphloroglucinol Acetyltransferase from Pseudomonas sp. YGJ3
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概要
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Monoacetylphloroglucinol (MAPG) acetyltransferase, catalyzing the conversion of MAPG to 2,4-diacetylphloroglucinol (DAPG), was purified from <I>Pseudomonas</I> sp. YGJ3 grown without Cl<SUP>−</SUP>. Cl<SUP>−</SUP> and pyoluteorin repressed expression of the enzyme. SDS-polyacrylamide gel electrophoresis showed that the purified enzyme (<I>M</I><SUB>r</SUB>=330 kDa) was composed of three subunits of 17, 38, and 43 kDa, and protein sequencing identified these as PhlB, PhlA, and PhlC respectively. The enzyme catalyzed the reversible disproportionation of 2 moles of MAPG to phloroglucinol (PG) and DAPG. The equilibrium constant <I>K</I> (=[DAPG][PG]/[MAPG]<SUP>2</SUP>) was estimated to be about 1.0 at 25 °C. A <I>Kpn</I>I 20-kb DNA fragment was cloned from the genomic DNA of strain YGJ3, and a 12,598-bp long DNA region containing the <I>phl</I> gene cluster <I>phlACBDEFGHI</I> was sequenced. PCR cloning and expression of the <I>phl</I> genes in <I>Escherichia coli</I> confirmed that expression of <I>phlACB</I> genes produced MAPG ATase.
- 2012-03-23
著者
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Maruyama Kiyofumi
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Sugisaki Hiroyuki
Institute For Chemical Research Kyoto University
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Matano Ikue
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Saitou Hiroki
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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HAYASHI Asuka
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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MORI Tomomi
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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Mori Tomomi
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Hayashi Asuka
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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