Identification of mutation sites on ω3 desaturase genes from Mortierella alpina 1S-4 mutants

Journal of Bioscience and Bioengineering

Volumn 107, Issue 1, 2009, Pages 7-9

  Sakuradani, Eiji ^a   Abe, Takahiro ^a   Shimizu, Sakayu ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

3 desaturase; Filamentous fungus; Mortierella alpina; Mutant; Mutation site; Polyunsaturated fatty acid

Indexed keywords

FILAMENTOUS FUNGUS; MORTIERELLA ALPINA; MUTANT; MUTATION SITE; POLYUNSATURATED FATTY ACID;

AMINES; AMINO ACIDS; GENES; ORGANIC ACIDS;

FATTY ACIDS;

ARACHIDONIC ACID; DNA MUTATIONAL ANALYSIS; FATTY ACID DESATURASES; FATTY ACIDS; FATTY ACIDS, UNSATURATED; ISOENZYMES; MODELS, BIOLOGICAL; MODELS, GENETIC; MORTIERELLA; MUTATION; TEMPERATURE; TIME FACTORS;

FUNGI; MORTIERELLA ALPINA;

EID: 58149301479     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2008.08.001     Document Type: Article

References (13)

1. Carlson S.E., Werkman S.H., Peeples J.M., Cooke R.J., and Tolley E.A. Arachidonic acid status correlates with first year growth in preterm infants. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 1073-1077
2. Shimokawa H. Beneficial effects of eicosapentaenoic acid on endothelial vasodilator functions in animals and humans. World Rev. Nutr. Diet 88 (2001) 100-108
3. Mori T.A., Beilin L.J., Burke V., Morris J., and Ritchie J. Interactions between dietary fat, fish, and fish oils and their effects on platelet function in men at risk of cardiovascular disease. Arterioscler. Thromb. Vasc. Biol. 17 (1997) 279-286
4. Yamada H., Shimizu S., and Shinmen Y. Production of arachidonic acid by Mortierella elongata 1S-5. Agric. Biol. Chem. 51 (1987) 785-790
5. Shimizu S., Shinmen Y., Kawashima H., Akimoto K., and Yamada H. Fungal mycelia as a novel source of eicosapentaenoic acid. Activation of enzyme(s) involved in eicosapentaenoic acid production at low temperature. Biochim. Biophys. Res. Commun. 150 (1988) 335-341
6. Jareonkitmongkol S., Shimizu S., and Yamada H. Fatty acid desaturation-defective mutants of an arachidonic-acid-producing fungus, Mortierella alpina 1S-4. J. Gen. Microbiol. 138 (1992) 997-1002
7. Jareonkitmongkol S., Sakuradani E., and Shimizu S. Isolation and characterization of an ω3-desaturation-defective mutant of an arachidonic acid-producing fungus. Arch. Microbiol. 161 (1994) 316-319
8. Sakuradani E., Hirano Y., Kamada N., Nojiri M., Ogawa J., and Shimizu S. Improvement of arachidonic acid production by mutants with lower n-3 desaturation activity derived from Mortierella alpina 1S-4. Appl. Microbiol. Biotechnol. 66 (2004) 243-248
9. Abe T., Sakuradani E., Asano T., Kanamaru H., and Shimizu S. Functional characterization of Δ9 and ω9 desaturase genes in Mortierella alpina 1S-4 and its derivative mutants. Appl. Microbiol. Biotechnol. 70 (2006) 711-719
10. Abe T., Sakuradani E., Asano T., Kanamaru H., Ioka Y., and Shimizu S. Identification of mutation sites on Δ6 desaturase genes from Mortierella alpina 1S-4 mutants. Biosci. Biotechnol. Biochem. 69 (2005) 1021-1024
11. Abe T., Sakuradani E., Ueda T., and Shimizu S. Identification of mutation sites on Δ5 desaturase genes from Mortierella alpina 1S-4 mutants. J. Biosci. Bioeng. 99 (2005) 296-299
12. Jareonkitmongkol S., Kawashima H., Shirasaka N., Shimizu S., and Yamada H. Production of dihomo-γ-linolenic acid by a Δ5-desaturase-defective mutant of Mortierella alpina 1S-4. Appl. Environ. Microbiol. 58 (1992) 2196-2200
13. Shanklin J., Whittle E., and Fox B.G. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33 (1994) 12787-12794