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Papers In Press, published online ahead of print December 23, 2002
Cardiff School of Biosciences, Cardiff University, Cardiff CF10 3TL
Corresponding Author: Dickinson{at}cardiff.ac.uk
The catabolism of phenylalanine to 2-phenylethanol and of tryptophan to tryptophol were studied by 13C NMR spectroscopy and GC-MS. Phenylalanine and tryptophan are first de-aminated (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 which comprises Pdc1p, Pdc5p, Pdc6p, Ydl080cp and Ydr380wp. Using strains containing all possible combinations of mutations affecting the 7 AAD genes (putative aryl alcohol dehydrogenases), 5 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.)
J. Biol. Chem, 10.1074/jbc.M211914200
Submitted on November 22, 2002
Revised on December 17, 2002
Accepted on December 23, 2002
The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae
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