CELL-FREE SYNTHESIS OF ETHYL ACETATE BY EXTRACTS FROM<i>SACCHAROMYCES CEREVISIAE</i>

Howard, Deborah; Anderson, R. G.

doi:10.1002/j.2050-0416.1976.tb03728.x

Cited by 48 publications

(13 citation statements)

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“…Esters arise from a reaction between an alcohol, which may be ethanol or of longer chain-length and a fatty acyl-CoA ester. The reaction is catalysed by an alcohol acetyl transferase (Howard and Anderson, 1976), which is probably located within subcellular structures termed vacuomes (Malcorps and Dufour, 1987). The acyl component of the activated fatty acid may be acetate, produced by the action of pyruvate dehydrogenase.…”

Section: Estersmentioning

confidence: 99%

4 Developments in Brewery Fermentation

1991

Biotechnology and Genetic Engineering Reviews

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Section: Estersmentioning

confidence: 99%

4 Developments in Brewery Fermentation

1991

Biotechnology and Genetic Engineering Reviews

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“…Early biochemical studies isolated Atf activity from microsomal cell fractions [4], [17] and C-terminal GFP-tagged Atf1 confirmed LD localization by Nile Red co-staining [18]. High throughput screening suggests ER localization of both Atf1 and −2 [19].…”

Section: Introductionmentioning

confidence: 96%

Dual N- and C-Terminal Helices Are Required for Endoplasmic Reticulum and Lipid Droplet Association of Alcohol Acetyltransferases in Saccharomyces cerevisiae

Lin

Wheeldon

2014

PLoS ONE

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In the yeast Saccharomyces cerevisiae two alcohol acetyltransferases (AATases), Atf1 and Atf2, condense short chain alcohols with acetyl-CoA to produce volatile acetate esters. Such esters are, in large part, responsible for the distinctive flavors and aromas of fermented beverages including beer, wine, and sake. Atf1 and Atf2 localize to the endoplasmic reticulum (ER) and Atf1 is known to localize to lipid droplets (LDs). The mechanism and function of these localizations are unknown. Here, we investigate potential mechanisms of Atf1 and Atf2 membrane association. Segments of the N- and C-terminal domains of Atf1 (residues 24–41 and 508–525, respectively) are predicted to be amphipathic helices. Truncations of these helices revealed that the terminal domains are essential for ER and LD association. Moreover, mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix disrupted ER association and subsequent sorting from the ER to LDs. Similar amphipathic helices are found at both ends of Atf2, enabling ER and LD association. As was the case with Atf1, mutations to the N- and C-terminal helices of Atf2 prevented membrane association. Sequence comparison of the AATases from Saccharomyces, non-Saccharomyces yeast (K. lactis and P. anomala) and fruits species (C. melo and S. lycopersicum) showed that only AATases from Saccharomyces evolved terminal amphipathic helices. Heterologous expression of these orthologs in S. cerevisiae revealed that the absence of terminal amphipathic helices eliminates LD association. Combined, the results of this study suggest a common mechanism of membrane association for AATases via dual N- and C-terminal amphipathic helices.

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“…The culture supernatant was obtained by centrifugation and its flavor components, i.e., i-AmOH, i-AmOAc, and isobutyl alcohol (i-BuOH) were detected by head space gas chromatography. 2 7,28) Amino acid Starvation Glu case (1) a-isopropylmalate synthase (LEU4); (2) …”

Section: /Isoamyl Acetatelmentioning

confidence: 99%