Abstract: The invention relates to at least one nucleotide sequence, derived from a nucleotide sequence encoding an acyltransferase polypeptide comprising at least one membrane-spanning region, encoding an improved active membrane independent acyltransferase polypeptide in which at least one amino acid residue of the membrane-spanning region has been deleted and/or substituted as compared to the original acyltransferase polypeptide, wherein the encoded active membrane independent acyltransferase polypeptide can produce fatty acid esters and/or fatty acid thioesters such as triacylglycerols, diacylglycerols, monoacylglycerols, phospholipids, glycolipids, waxesters, acylated carbohydrates, acylated amino acids, and lysolipids, e.g. lysophosphospholipid, lysolecithin. Thereby one single acyltransferase can be used for the production of a huge number of products.

Abstract: The invention relates to at least one nucleotide sequence, derived from a nucleotide sequence encoding an acyltransferase polypeptide comprising at least one membrane-spanning region, encoding an improved active membrane independent acyltransferase polypeptide in which at least one amino acid residue of the membrane-spanning region has been deleted and/or substituted as compared to the original acyltransferase polypeptide, wherein the encoded active membrane independent acyltransferase polypeptide can produce fatty acid esters and/or fatty acid thioesters such as triacylglycerols, diacylglycerols, monoacylglycerols, phospholipids, glycolipids, waxesters, acylated carbohydrates, acylated amino acids, and lysolipids, e.g. lysophosphospholipid, lysolecithin. Thereby one single acyltransferase can be used for the production of a huge number of products.

Abstract: Disclosed is a method for modifying the chain length and double bond positional specificities of a soluble plant fatty acid desaturase. More specifically, the method involves modifying amino acid contact residues in the substrate binding channel of the soluble fatty acid desaturase which contact the fatty acid. Specifically disclosed is the modification of an acyl-ACP desaturase. Amino acid contact residues which lie within the substrate binding channel are identified, and subsequently replaced with different residues to effect the modification of activity.