The soybean (Glycine max) was modified for increased levels of monounsaturated fatty acid (oleic) and decreased levels of polyunsaturated fatty acids (linoleic and linolenic). The LM soybean was also modified for tolerance to sulfonylurea herbicides in order to be used as a marker selection for transformants. To achieve this trait, the soybean expresses the modified Glycine max microsomal omega-6 desaturase gene (fad2-1) where the fragment of the fad2-1 gene does not code for a protein and silences the expression of the endogenous soybean omega-6 desaturase, resulting in accumulated monounsaturated fats. For the selectable marker, to achieve tolerance to sulfonylurea, the soybean expresses the modified acetolactate synthase (als) gene from Glycine max (hra) which is a variant of the acetolactate synthase enzyme derived from Glycine max (also known as acetohydroxy acid synthase). Acetohydroxy acid synthase (also known as acetolactate synthase)  is a key enzyme that catalyzes the first common step in the biosynthesis of the essential branched-chain amino acids isoleucine, leucine, and valine. This protein contains two mutations in its amino acid sequence that reduce binding affinity to ALS-inhibiting herbicides and thus are responsible for GM-HRA resistance to ALS-inhibiting herbicides (e.g., sulfonylureas and triazolopyrimidines).