Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli

Fukuda, Katsuhiko; Kiyokawa, Yoshifumi; Yanagiuchi, Toshiyasu; Wakai, Yoshinori; Kitamoto, Katsuhiko; Inoue, Yoshiharu; Kimura, Akira

doi:10.1007/s002530051662

Cited by 57 publications

(34 citation statements)

References 17 publications

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“…Sequence comparisons suggest that these ORFs encode proteins most closely related to the C-terminal halves of the ORF1 proteins of several vertebrate members of the CR1 clade of non-LTR retrotransposons, such as CR1 from the chicken (34) and Maui from the pufferfish Fugu rubripes (35). As has been noted by Kapitonov and Jurka (36), the ORF1 proteins of these non-LTR retrotransposons are related to a variety of cellular enzymes, including TEP-I (thioesterase) from E. coli (37), brain platelet-activating factor acetyl hydrolase (PAF-AH) from the cow (38), and the isoamyl acetate-hydrolyzing esterase (IAH1) from Saccharomyces cerevisiae (39). Several of these related enzymes, including brain PAF-AH (38) and TEP-I (37), have been experimentally characterized and found to possess catalytic triads containing conserved serine, aspartate, and histidine residues.…”

Section: Ngaro Elements Encode a Putative Hydrolasementioning

confidence: 93%

Tyrosine Recombinase Retrotransposons and Transposons

Poulter

Butler

2015

Microbiol Spectr

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Retrotransposons carrying tyrosine recombinases (YR) are widespread in eukaryotes. The first described tyrosine recombinase mobile element, DIRS1, is a retroelement from the slime mold Dictyostelium discoideum. The YR elements are bordered by terminal repeats related to their replication via free circular dsDNA intermediates. Site-specific recombination is believed to integrate the circle without creating duplications of the target sites. Recently a large number of YR retrotransposons have been described, including elements from fungi (mucorales and basidiomycetes), plants (green algae) and a wide range of animals including nematodes, insects, sea urchins, fish, amphibia and reptiles. YR retrotransposons can be divided into three major groups: the DIRS elements, PAT-like and the Ngaro elements. The three groups form distinct clades on phylogenetic trees based on alignments of reverse transcriptase/ribonuclease H (RT/RH) and YR sequences, and also having some structural distinctions. A group of eukaryote DNA transposons, cryptons, also carry tyrosine recombinases. These DNA transposons do not encode a reverse transcriptase. They have been detected in several pathogenic fungi and oomycetes. Sequence comparisons suggest that the crypton YRs are related to those of the YR retrotransposons. We suggest that the YR retrotransposons arose from the combination of a crypton-like YR DNA transposon and the RT/RH encoding sequence of a retrotransposon. This acquisition must have occurred at a very early point in the evolution of eukaryotes.

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Section: Ngaro Elements Encode a Putative Hydrolasementioning

confidence: 93%

Tyrosine Recombinase Retrotransposons and Transposons

Poulter

Butler

2015

Microbiol Spectr

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“…As esterases are responsible for the breakdown of esters, it is clear that their activity may affect the concentration of certain volatile esters. In S. cerevisiae, for example, it has been shown that the balance between ester-synthesizing enzymes and esterases, such as Iah1p (also known as Est2p), is important for the net rate of ester accumulation (27)(28)(29)(30) (59,60,61,62,70). This indicates that esterases may also play a role in the formation of certain esters (42,62,70).…”

Section: Discussionmentioning

confidence: 99%

Expression Levels of the Yeast Alcohol Acetyltransferase GenesATF1,Lg-ATF1, andATF2Control the Formation of a Broad Range of Volatile Esters

Verstrepen

Laere

Vanderhaegen

et al. 2003

Appl Environ Microbiol

336

322

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Volatile aroma-active esters are responsible for the fruity character of fermented alcoholic beverages such as beer and wine. Esters are produced by fermenting yeast cells in an enzyme-catalyzed intracellular reaction. In order to investigate and compare the roles of the known Saccharomyces cerevisiae alcohol acetyltransferases, Atf1p, Atf2p and Lg-Atf1p, in volatile ester production, the respective genes were either deleted or overexpressed in a laboratory strain and a commercial brewing strain. Subsequently, the ester formation of the transformants was monitored by headspace gas chromatography and gas chromatography combined with mass spectroscopy (GC-MS). Analysis of the fermentation products confirmed that the expression levels of ATF1 and ATF2 greatly affect the production of ethyl acetate and isoamyl acetate. GC-MS analysis revealed that Atf1p and Atf2p are also responsible for the formation of a broad range of less volatile esters, such as propyl acetate, isobutyl acetate, pentyl acetate, hexyl acetate, heptyl acetate, octyl acetate, and phenyl ethyl acetate. With respect to the esters analyzed in this study, Atf2p seemed to play only a minor role compared to Atf1p. The atf1⌬ atf2⌬ double deletion strain did not form any isoamyl acetate, showing that together, Atf1p and Atf2p are responsible for the total cellular isoamyl alcohol acetyltransferase activity. However, the double deletion strain still produced considerable amounts of certain other esters, such as ethyl acetate (50% of the wild-type strain), propyl acetate (50%), and isobutyl acetate (40%), which provides evidence for the existence of additional, as-yet-unknown ester synthases in the yeast proteome. Interestingly, overexpression of different alleles of ATF1 and ATF2 led to different ester production rates, indicating that differences in the aroma profiles of yeast strains may be partially due to mutations in their ATF genes.During fermentation processes, yeast cells produce a broad range of aroma-active substances which greatly affect the complex flavor of fermented alcoholic beverages. While these secondary metabolites are often formed only in trace amounts, their concentrations determine the distinct aroma of these beverages. Flavor-active substances produced by fermenting yeast cells can be divided into five main groups: sulfur-containing molecules, organic acids, higher alcohols, carbonyl compounds, and volatile esters (32,39,56,57,66). Of these categories, volatile esters represent the largest and most important group. They are responsible for the highly desired fruity character of beer and, to a lesser extent, other alcoholic beverages, such as wine.The major flavor-active esters in beer are acetate esters such as ethyl acetate (solvent-like aroma), isoamyl acetate (banana flavor), and phenylethyl acetate (flowery, rose aroma). In addition, C 6 -C 10 medium-chain fatty acid ethyl esters such as ethyl hexanoate (ethyl caproate) and ethyl octanoate (ethyl caprylate), which have "sour apple" aromas, are also important for the overall bouqu...

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“…While extensive research has been carried out on the enzymes responsible for ester formation by wine strains of Saccharomyces cerevisiae (22,23,45,51), esterase activity for winerelated LAB is not well documented. Most characterization of esterases in LAB has focused on dairy isolates (9,(16)(17)(18)20).…”

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confidence: 99%

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Sumby

Matthews

Grbin

et al. 2009

Appl Environ Microbiol

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We report the cloning and characterization of EstB28, the first esterase to be so characterized from the wine-associated lactic acid bacterium, Oenococcus oeni. The published sequence for O. oeni strain PSU-1 was used to identify putative esterase genes and design PCR primers in order to amplify the corresponding region from strain Ooeni28, an isolate intended for inoculation of wines. In this way a 912-bp open reading frame (ORF) encoding a putative esterase of 34.5 kDa was obtained. The amino acid sequence indicated that EstB28 is a member of family IV of lipolytic enzymes and contains the GDSAG motif common to other lactic acid bacteria. This ORF was cloned into Escherichia coli using an appropriate expression system, and the recombinant esterase was purified. Characterization of EstB28 revealed that the optimum temperature, pH, and ethanol concentration were 40°C, pH 5.0, and 28% (vol/vol), respectively. EstB28 also retained marked activity under conditions relevant to winemaking (10 to 20°C, pH 3.5, 14% [vol/vol] ethanol). Kinetic constants were determined for EstB28 with p-nitrophenyl (pNP)-linked substrates ranging in chain length from C 2 to C 18 . EstB28 exhibited greatest specificity for C 2 to C 4 pNP-linked substrates.

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Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli

Cited by 57 publications

References 17 publications

Tyrosine Recombinase Retrotransposons and Transposons

Tyrosine Recombinase Retrotransposons and Transposons

Expression Levels of the Yeast Alcohol Acetyltransferase GenesATF1,Lg-ATF1, andATF2Control the Formation of a Broad Range of Volatile Esters

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

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