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Abstract:
The enormous diversity of terpenes found in nature is generated by enzymes known as terpene synthases, or cyclases.
Some are also known for their ability to convert a single substrate into multiple products. This review comprises
monoterpene and sesquiterpene synthases that are multiproduct in nature along with the regulation factors that can
alter the product specificity of multiproduct terpene synthases without genetic mutations. Variations in specific assay
conditions with focus on shifts in product specificity based on change in metal cofactors, assay pH and substrate geometry
are described. Alterations in these simple cellular conditions provide the organism with enahnced chemodiversity without
investing into new enzymatic architecture. This versatility to modulate product diversity grants organisms, especially
immobile ones like plants with access to an enhanced defensive repertoire by simply altering cofactors, pH level and
substrate geometry.
