Aliphatic glucosinolates are a major class of defensive secondary metabolites in plants that are mostly derived from methionine. Occurring in different chain lengths, they show a structural diversity arising from the variable number of chain elongation cycles taking place during their biosynthesis. The key enzymes in determining glucosinolate chain length are the methylthioalkylmalate (MAM) synthases, MAM1 and MAM3, with MAM3 showing a broader substrate specificity than MAM1. A comparison of the measurements of wild type and MAM1 knockout mutant plants shows the following distinct changes in glucosinolate chain length profiles:

(1)	a reversal of the relative proportions of the two shortest glucosinolates,
(2)	a significant increase in the concentration of the longest glucosinolate,
(3)	an increase in total glucosinolate content in the mutant.

MAM3 knockout mutants on the contrary differ from wild type plants by a pronounced abundance of the second shortest glucosinolate and the depletion of the two longest glucosinolates. To clarify the contribution of the multifunctional enzymes MAM1 and MAM3 to the glucosinolate profile of Arabidopsis thaliana leaves, we simulated glucosinolate biosynthesis in a kinetic model, taking into account the structure of the pathway and measured enzymatic properties. The predicted glucosinolate profiles show all characteristics of the actual differences between wild-type and MAM1 mutants or MAM3 mutants, respectively. The model strongly supports experimental indications that the two MAM activities are not independent of each other. In particular, it showed that an elevated expression of MAM3 in the MAM1 mutant is critical in determining the glucosinolate profile of this plant line. The simulation was critical for this finding since it allowed us to assess the individual effects of two processes—the knocking out of MAM1 and the overexpression of MAM3—that are difficult to separate experimentally.