Über <i>p</i>‐Aminophenylarsinsäure

Ehrlich, Peter F.; Bertheim, A.

doi:10.1002/cber.19070400397

Cited by 72 publications

(31 citation statements)

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“…In S. cerevisiae catabolism of the three branched-chain amino acids (leucine, valine, and isoleucine) and the two aromatic amino acids (phenylalanine and tryptophan) proceeds essentially as Ehrlich proposed nearly 100 years ago (28). However, it is much more complex than Ehrlich ever imagined, because yeast uses at least three aminotransferases, five decarboxylases, and six alcohol dehydrogenases.…”

Section: Discussionmentioning

confidence: 99%

The Catabolism of Amino Acids to Long Chain and Complex Alcohols in Saccharomyces cerevisiae

Dickinson

Salgado

Hewlins

2003

Journal of Biological Chemistry

307

249

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The catabolism of phenylalanine to 2-phenylethanol and of tryptophan to tryptophol were studied by 13 C NMR spectroscopy and gas chromatography-mass spectrometry. Phenylalanine and tryptophan are first deaminated (to 3-phenylpyruvate and 3-indolepyruvate, respectively) and then decarboxylated. This decarboxylation can be effected by any of Pdc1p, Pdc5p, Pdc6p, or Ydr380wp; Ydl080cp has no role in the catabolism of either amino acid. We also report that in leucine catabolism Ydr380wp is the minor decarboxylase. Hence, all amino acid catabolic pathways studied to date use a subtly different spectrum of decarboxylases from the five-membered family that comprises Pdc1p, Pdc5p, Pdc6p, Ydl080cp, and Ydr380wp. Using strains containing all possible combinations of mutations affecting the seven AAD genes (putative aryl alcohol dehydrogenases), five ADH genes, and SFA1, showed that the final step of amino acid catabolism (conversion of an aldehyde to a long chain or complex alcohol) can be accomplished by any one of the ethanol dehydrogenases (Adh1p, Adh2p, Adh3p, Adh4p, Adh5p) or by Sfa1p (formaldehyde dehydrogenase.)

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Section: Discussionmentioning

confidence: 99%

The Catabolism of Amino Acids to Long Chain and Complex Alcohols in Saccharomyces cerevisiae

Dickinson

Salgado

Hewlins

2003

Journal of Biological Chemistry

307

249

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“…For studies of valine catabolism cells were grown in minimal medium containing (per liter) 1.67 g of yeast nitrogen base (Difco), 20 g of valine, and either 20 ml of ethanol or 20 g of glucose for the carbon source. Experiments involving 13 C labeling used [2][3][4][5][6][7][8][9][10][11][12][13] C]valine (99.9 atom %) from Cambridge Isotope Laboratories (Cambridge, MA). Auxotrophic requirements were supplied as required at 20 g/ml.…”

Section: Methodsmentioning

confidence: 99%

“…The predominant view, until our recent work on leucine catabolism (1), has been that yeasts first use transamination, but that decarboxylation of the keto acids proceeds via a "carboxylase" to an aldehyde that is then reduced in an NADH-linked reaction producing the appropriate "fusel" alcohol (3)(4)(5). This explanation, sometimes called the "Ehrlich pathway" to honor the originator of the ideas (6), which were slightly modified later (7), has numerous problems. The Ehrlich pathway has never been properly proven as the route by which the branched-chain amino acids are catabolized in yeasts.…”

mentioning

confidence: 99%

An Investigation of the Metabolism of Valine to Isobutyl Alcohol in Saccharomyces cerevisiae

Dickinson¹,

Harrison²,

Hewlins³

1998

Journal of Biological Chemistry

165

136

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The metabolism of valine to isobutyl alcohol in yeast was examined by 13 C nuclear magnetic resonance spectroscopy and combined gas chromatography-mass spectrometry. The product of valine transamination, ␣-ketoisovalerate, had four potential routes to isobutyl alcohol. The first, via branched-chain ␣-ketoacid dehydrogenase to isobutyryl-CoA is not required for the synthesis of isobutyl alcohol because abolition of branchedchain ␣-ketoacid dehydrogenase activity in an lpd1 disruption mutant did not prevent the formation of isobutyl alcohol. The second route, via pyruvate decarboxylase, is the one that is used because elimination of pyruvate decarboxylase activity in a pdc1 pdc5 pdc6 triple mutant virtually abolished isobutyl alcohol production. A third potential route involved ␣-ketoisovalerate reductase, but this had no role in the formation of isobutyl alcohol from ␣-hydroxyisovalerate because cell homogenates could not convert ␣-hydroxyisovalerate to isobutyl alcohol. The final possibility, use of the pyruvate decarboxylase-like enzyme encoded by YDL080c, seemed to be irrelevant, because a strain with a disruption in this gene produced wild-type levels of isobutyl alcohol. Thus there are major differences in the catabolism of leucine and valine to their respective "fusel" alcohols. Whereas in the catabolism of leucine to isoamyl alcohol the major route is via the decarboxylase encoded by YDL080c, any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine. Finally, analysis of the 13 C-labeled products revealed that the pathways of valine catabolism and leucine biosynthesis share a common pool of ␣-ketoisovalerate.

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“…The decomposition and conversion is carried out according to the Ehrlich metabolic pathway [4]. The values ranged from 2.8 to 9.8 mg/l.…”

Section: Resultsmentioning

confidence: 99%

Influence of different yeasts on the amino acid pattern of rosé wine

et al. 2017

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Abstract. In an experiment with Rosé wine, 27 different commercial yeasts were tested for their influence on the amino acid pattern of the wine. Amino acids are precursors for aromatic substances; therefore a large variation of the amino acid values in the wine was expected. Blaufränkisch grapes with 20 • KMW were matured in the cellar with 27 different commercial yeasts. The fermentation was carried out in 34l vessels. The wines were measured for amino acids using an HP 1200 liquid chromatograph and HP-FLD1100 according to Umagat. The wines showed 13.5% alcohol and little residual sugar. The measurement results of the amino acids of the different wines showed large variations. For example, the amount of the amino acid alanine in wine varied from 17 to 138 mg. In particular, the wines of the yeast Pino Type showed the highest amounts of alanine in comparison to the other fermented wines.

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Über p‐Aminophenylarsinsäure

Cited by 72 publications

References 0 publications

The Catabolism of Amino Acids to Long Chain and Complex Alcohols in Saccharomyces cerevisiae

The Catabolism of Amino Acids to Long Chain and Complex Alcohols in Saccharomyces cerevisiae

An Investigation of the Metabolism of Valine to Isobutyl Alcohol in Saccharomyces cerevisiae

Influence of different yeasts on the amino acid pattern of rosé wine

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