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Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme
Author(s) -
Katavic Vesna,
Barton Dennis L.,
Giblin E.Michael,
Reed Darwin W.,
Kumar Arvind,
Taylor David C.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00198-x
Subject(s) - serine , enzyme , chemistry , biochemistry , yeast , yield (engineering) , fatty acid , amino acid , residue (chemistry) , materials science , metallurgy
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.