Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.
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.
Katavic
Vesna
V
CanAmera Foods/Bunge at Plant Biotechnology Institute, P.O. Box 479, 125 Willow Court, Osler, SK, Canada S0K 3A0. vesna.katavic@nrc.ca
Barton
Dennis L
DL
Giblin
E Michael
EM
Reed
Darwin W
DW
Kumar
Arvind
A
Taylor
David C
DC
D000123:Acetyltransferases / Q000235:genetics* / Q000378:metabolism*; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D029688:Brassica napus / Q000201:enzymology* / Q000235:genetics; D000081031:Fatty Acid Elongases; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism*; D012694:Serine / Q000378:metabolism*
D000596:Amino Acids; D010940:Plant Proteins; D012694:Serine; D000123:Acetyltransferases; D000081031:Fatty Acid Elongases