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J. Biol. Chem., Vol. 278, Issue 10, 8028-8034, March 7, 2003
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From the The catabolism of phenylalanine to
2-phenylethanol and of tryptophan to tryptophol were studied by
13C 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.)
The Catabolism of Amino Acids to Long Chain and Complex Alcohols
in Saccharomyces cerevisiae*
§,, and Cardiff School of Biosciences, Cardiff
University, CF10 3TL Cardiff and the ¶ Department of Chemistry,
Cardiff University, CF10 3TB Cardiff, United Kingdom
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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