1887

Abstract

-Butyrolactones play an important role in the regulation of antibiotic production and differentiation in . However the biosynthetic pathway for these small molecules has not yet been determined, and synthesis has not been reported. The function of the AfsA family of proteins, originally proposed to catalyse -butyrolactone synthesis, has been in debate. To clarify the function of the AfsA family, and to understand the synthesis of the -butyrolactones, we performed analysis of this protein family. AfsA proteins consist of two divergent domains, each of which has similarity to the fatty acid synthesis enzymes FabA and FabZ. The two predicted active sites in ScbA, which is the AfsA orthologue found in , were mutated, and -butyrolactone biosynthesis was abolished in all four constructed mutants, strongly suggesting that ScbA has enzymic activity.

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2007-05-01
2019-10-19
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A. (a) Base peak chromatogram of M145::pSET152. (b) Extracted ion chromatogram (SIM) for / 245 ([244+H] ) of sample M145::pSET152. (c) Base peak chromatogram of SCB1 standard. (B) (a) Mass spectrum of the peak at retention time 14.5 min of sample M145::pSET152. (b) Mass spectrum of SCB1 standard. (c) MS/MS spectrum of the / 245 hydrogen adduct, peak at 14.5 min of sample M145::pSET152. (d) MS/MS spectrum of the / 245 hydrogen adduct, SCB1 standard.

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A. (a) Base peak chromatogram of sample M751::pIJ6147. (b) Extracted ion chromatogram (SIM) for / 245 ([244+H] ) of sample M751::pIJ6147. (c) Base peak chromatogram of SCB1 standard. B. (a) Mass spectrum of the peak at retention time 14.5 min of sample M751::pIJ6147. (b) Mass spectrum of SCB1 standard.

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Full descriptions of the contruction of ScbA mutants are available here.

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