Functional roles and substrate specificities of twelve cytochromes P450 belonging to CYP52 family in n-alkane assimilating yeast Yarrowia lipolytica
| Autor: | Chiaki Ishimaru, Satoshi Kobayashi, Ryo Iwama, Akinori Ohta, Ryouichi Fukuda, Hiroyuki Horiuchi |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Yarrowia Aldehyde dehydrogenase Microbiology Substrate Specificity 03 medical and health sciences Fatty aldehyde chemistry.chemical_compound Cytochrome P-450 Enzyme System hemic and lymphatic diseases Alkanes Genetics chemistry.chemical_classification Aldehydes biology Fatty acid metabolism Fatty Acids Fatty acid Cytochrome P450 Aldehyde Dehydrogenase Dodecanal biology.organism_classification Yeast 030104 developmental biology Biochemistry chemistry biology.protein Fatty Alcohols Oxidation-Reduction Gene Deletion |
| Zdroj: | Fungal Genetics and Biology. 91:43-54 |
| ISSN: | 1087-1845 |
| DOI: | 10.1016/j.fgb.2016.03.007 |
| Popis: | Yarrowia lipolytica possesses twelve ALK genes, which encode cytochromes P450 in the CYP52 family. In this study, using a Y. lipolytica strain from which all twelve ALK genes had been deleted, strains individually expressing each of the ALK genes were constructed and their roles and substrate specificities were determined by observing their growth on n-alkanes and analyzing fatty acid metabolism. The results suggested that the twelve Alk proteins can be categorized into four groups based on their substrate specificity: Alk1p, Alk2p, Alk9p, and Alk10p, which have significant activities to hydroxylate n-alkanes; Alk4p, Alk5p, and Alk7p, which have significant activities to hydroxylate the ω-terminal end of dodecanoic acid; Alk3p and Alk6p, which have significant activities to hydroxylate both n-alkanes and dodecanoic acid; and Alk8p, Alk11p, and Alk12p, which showed faint or no activities to oxidize these substrates. The involvement of Alk proteins in the oxidation of fatty alcohols and fatty aldehydes was also analyzed by measuring viability of the mutant deleted for twelve ALK genes in medium containing dodecanol and by observing growth on dodecanal of a mutant strain, in which twelve ALK genes were deleted along with four fatty aldehyde dehydrogenase genes. It was suggested that ALK gene(s) is/are involved in the detoxification of dodecanol and the assimilation of dodecanal. These results imply that genes encoding CYP52-family P450s have undergone multiplication and diversification in Y. lipolytica for assimilation of various hydrophobic compounds. |
| Databáze: | OpenAIRE |
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