The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The biochemistry of peroxisomal β-oxidation in the yeast Saccharomyces cerevisiae
Abstract
Peroxisomal fatty acid degradation in the yeast Saccharomyces cerevisiae requires an array of beta-oxidation enzyme activities as well as a set of auxiliary activities to provide the beta-oxidation machinery with the proper substrates. The corresponding classical and auxiliary enzymes of beta-oxidation have been completely characterized, many at the structural level with the identification of catalytic residues. Import of fatty acids from the growth medium involves passive diffusion in combination with an active, protein-mediated component that includes acyl-CoA ligases, illustrating the intimate linkage between fatty acid import and activation. The main factors involved in protein import into peroxisomes are also known, but only one peroxisomal metabolite transporter has been characterized in detail, Ant1p, which exchanges intraperoxisomal AMP with cytosolic ATP. The other known transporter is Pxa1p-Pxa2p, which bears similarity to the human adrenoleukodystrophy protein ALDP. The major players in the regulation of fatty acid-induced gene expression are Pip2p and Oaf1p, which unite to form a transcription factor that binds to oleate response elements in the promoter regions of genes encoding peroxisomal proteins. Adr1p, a transcription factor, binding upstream activating sequence 1, also regulates key genes involved in beta-oxidation. The development of new, postgenomic-era tools allows for the characterization of the entire transcriptome involved in beta-oxidation and will facilitate the identification of novel proteins as well as the characterization of protein families involved in this process.
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Cites
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
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Peroxisomes (microbodies and related particles).
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Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
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Transport of fatty acids and metabolites across the peroxisomal membrane
Hettema, E. H., & Tabak, H. F. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(00)00045-7 · Cited by 126
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Self-citation
Cited by
A Fungal Family of Transcriptional Regulators: the Zinc Cluster Proteins
MacPherson, S., Larochelle, M., & Turcotte, B. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00015-06 · Cited by 612
Peroxisomal β-oxidation—A metabolic pathway with multiple functions
Poirier, Y., Antonenkov, V. D., Glumoff, T., & Hiltunen, J. K. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.08.034 · Cited by 499
Self-citationThe lipid biochemistry of eukaryotic algae
Li-Beisson, Y., Thelen, J. J., Fedosejevs, E., & Harwood, J. L. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.01.003 · Cited by 453
Takahashi, H., McCaffery, J. M., Irizarry, R. A., & Boeke, J. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.040 · Cited by 438
Yeast lipid metabolism at a glance
Klug, L., & Daum, G. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12141 · Cited by 349
Metadata
- Authors
- Hiltunen, J. K., Mursula, A. M., Rottensteiner, H., Wierenga, R. K., Kastaniotis, A. J., & Gurvitz, A.
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-04
- Volume
- 27
- Issue
- 1
- Pages
- 35-64
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2128715992
- Cited by
- 348
- References
- 8
- FWCI
- 7.05
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hiltunen, J. K., Mursula, A. M., Rottensteiner, H., Wierenga, R. K., Kastaniotis, A. J., & Gurvitz, A. (2003). The biochemistry of peroxisomal β-oxidation in the yeast Saccharomyces cerevisiae. FEMS Microbiology Reviews. https://doi.org/10.1016/s0168-6445(03)00017-2
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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