The Ehrlich Pathway for Fusel Alcohol Production: a Century of Research on Saccharomyces cerevisiae Metabolism
- L. Hazelwood, J. Daran, A. V. van Maris, J. Pronk, J. Dickinson
- BiologyApplied and Environmental Microbiology
- 15 February 2008
Current scientific interest in the Ehrlich pathway is supported by increased demands for natural flavor compounds such as isoamyl alcohol and 2-phenylethanol, which can be produced from amino acids in yeast-based bioconversion processes, as well as by the need to control flavor profiles of fermented food products.
The metabolism and molecular physiology of Saccharomyces cerevisiae
- J. Dickinson, M. Schweizer
- Biology
- 9 December 1998
LIFE CYCLE AND MORPHOGENESIS J. Richard Dickinson MOTHER CELL-SPECIFIC AGEING Michael Breitenbach, Peter Laun, Gino Heeren, Stefanie Jarolim, and Alena Pichova CARBON METABOLISM Arthur Kruckeberg and…
The Catabolism of Amino Acids to Long Chain and Complex Alcohols in Saccharomyces cerevisiae *
- J. Dickinson, L. E. J. Salgado, M. Hewlins
- Biology, ChemistryJournal of Biological Chemistry
- 7 March 2003
Using strains containing all possible combinations of mutations affecting the seven AAD genes, fiveADH genes, and SFA1, it is shown that the final step of amino acid catabolism can be accomplished by any one of the ethanol dehydrogenases or by Sfa1p (formaldehyde dehydrogenase.)
Pharmaceutical Microbiology
- W. Hugo, J. Dickinson, A. Russell
- Biology
- 1 September 2006
This project seeks to demonstrate the importance of protease involvement in biofilm formation by S. epidermidis and to identify the proteases involved in the post-translational modification of Aap during this process.
A 13C Nuclear Magnetic Resonance Investigation of the Metabolism of Leucine to Isoamyl Alcohol in Saccharomyces cerevisiae *
- J. Dickinson, M. M. Lanterman, M. Hewlins
- BiologyJournal of Biological Chemistry
- 24 October 1997
The metabolism of leucine to isoamyl alcohol in yeast was examined by 13C nuclear magnetic resonance spectroscopy and it was found that a pyruvate decarboxylase-like enzyme encoded byYDL080c appears to be the major route of decar boxylation of α-ketoisocaproate to iso amyl alcohol although disruption of this gene reveals that at least one other unidentified decarboxesize can substitute to a minor extent.
An Investigation of the Metabolism of Valine to Isobutyl Alcohol in Saccharomyces cerevisiae *
- J. Dickinson, S. Harrison, M. Hewlins
- Biology, ChemistryJournal of Biological Chemistry
- 2 October 1998
Analysis of the 13C-labeled products revealed that the pathways of valine catabolism and leucine biosynthesis share a common pool of α-ketoisovalerate, and any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine.
Physiological Characterization of the ARO10-Dependent, Broad-Substrate-Specificity 2-Oxo Acid Decarboxylase Activity of Saccharomyces cerevisiae
- Z. Vuralhan, M. Luttik, J. Pronk
- BiologyApplied and Environmental Microbiology
- 1 June 2005
The results reported here indicate the involvement of posttranscriptional regulation and/or a second protein in the ARO10-dependent, broad-substrate-specificity decarboxylase activity.
Methionine catabolism in Saccharomyces cerevisiae.
- P. Perpète, Olivier Duthoit, J. Dickinson
- BiologyFEMS Yeast Research
- 2006
The catabolism of methionine to methionol and methanethiol in Saccharomyces cerevisiae was studied using (13)C NMR spectroscopy, GC-MS, enzyme assays and a number of mutants. Methionine is first…
'Fusel' alcohols induce hyphal-like extensions and pseudohyphal formation in yeasts.
- J. Dickinson
- BiologyMicrobiology
- 1 June 1996
Isoamyl alcohol induced the formation of pseudohyphae in two species of Candida and both hyphal-like extensions and pseudohYPHae in Brettanomyces anomalus, suggesting a close relationship or a common basis to the development of the two morphologies.
Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA.
- A. Alderson, P. Sabelli, Nigel G Halford
- BiologyProceedings of the National Academy of Sciences…
- 1 October 1991
A cDNA, cRKIN1, encoding a putative homologue of the yeast (Saccharomyces cerevisiae) SNF1-encoded protein-serine/threonine kinase, has been isolated from a library prepared from rye endosperm mRNA and its role in the control of carbon metabolism in endosperms of rye is suggested.
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