Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme

FEBS Letters

Giblin, E.Michael²  Kumar, Arvind¹  Reed, Darwin W.²  Katavic, Vesna¹  Barton, Dennis L.¹  Taylor, David C.² 

[1] CanAmera Foods/Bunge at Plant Biotechnology Institute, P.O. Box 479, 125 Willow Court, Osler, SK, Canada S0K 3A0;National Research Council of Canada, Plant Biotechnology Institute, 110 Gymnasium Place, Saskatoon, SK, Canada S7N 0W9

关键词: Fatty acid elongation 1;    Fatty acid elongase 1;    Site-directed mutagenesis;    Yeast expression;    Brassica;    Brassicaceae;    FAE1;    fatty acid elongase 1;    FAE1;    fatty acid elongation 1;    LEA;    low erucic acid;    VLCMFA;    very long chain monounsaturated fatty acid;    VLCFA;    very long chain fatty acid;    FAME;    fatty acid methyl esters;   

DOI  :  10.1016/S0014-5793(04)00198-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To gain some insight whether there is an absolute requirement for the serine 282 to yield a functional fatty acid elongase 1 condensing enzyme we have introduced point mutations in the FAE1 coding sequence which led to the substitution of serine 282 with several aliphatic or aromatic amino acids. The mutated FAE1 polypeptides were expressed in yeast. Gas chromatography analyses of the fatty acid methyl esters from yeast lysates and fatty acid elongase activity assays demonstrated that there is not an absolute requirement for serine at position 282 to yield a functional FAE1 condensing enzyme.

【 授权许可】

Unknown