Acyl-CoA oxidase, a key step for lipid accumulation in the yeast Yarrowia lipolytica
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002209" target="_blank" >RIV/61989592:15310/04:00002209 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Acyl-CoA oxidase, a key step for lipid accumulation in the yeast Yarrowia lipolytica
Original language description
The yeast Yarrowia lipolytica is able to use fatty acids as carbon source via P-oxidation. This yeast contains five acyl-CoA oxidases (Aoxps) encoded by POX genes. Two Aoxps are of particular interest: Aox2p, a medium chain oxidase, and Aox3p, an oxidasespecific for short chain substrates. To date, no 3D structure of these enzymes is available. To better understand their specificity, we have expressed 10 enzymes in Escherichia coli; Aox2p, Aox3p, a mutated Aox3 (Aox3mp), and seven chimera obtained by shuffling fragments of Aox2p and Aox3p (M1 to M4 and M6 to M8). Aox3mp and one chimeric protein (M6) were active, Aox3mp exhibited broad chain length specificity. We tested complementation of growth for strain MTLY36 (Deltapox2,3,5; reduced growth on oleic acid media) and MTLY40 (Deltapox2,3,4,5; not growing on oleic acid media) by expressing either Aox2p, Aox3p, Aox3mp, and M6 chimera encoding genes. We demonstrate that the POX genomic content affects both gamma-lactone production [J. Mo
Czech name
Acyl-CoA oxidasa, klíčový krok k akumulaci lipidů v kvasince Yarrowia lipolytica
Czech description
Článek diskutuje acyl-CoA oxidasa, jako klíčový krok k akumulaci lipidů v kvasince Yarrowia lipolytica.
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis B
ISSN
1381-1177
e-ISSN
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Volume of the periodical
28
Issue of the periodical within the volume
2-3
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
5
Pages from-to
81-85
UT code for WoS article
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EID of the result in the Scopus database
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