Natural Promiscuity Is at the Heart of Large Product Diversity

2 Natural Promiscuity Is at the Heart of Large Product Diversity 

Enzyme catalytic promiscuity, where enzymes catalyze not only reactions with their natural substrates but also with non-natural substrates, has begun to be recognized as a valuable research and synthesis tool [6-10, 12, 13]. In particular, the catalytic promiscuity displayed by sucrose-utilizing transglucosidases toward a wide range of acceptor molecules has started to be exploited to provide novel synthesis pathways that are currently not available. 

The main reaction catalyzed by these enzymes is the synthesis of extracellular bacterial polysaccharides, a-glucans linked through different types of linkages and harboring distinct sizes and strucmres depending on the enzyme specificity and producing strain (Tables 1 and 2). Polymer elongation has been shown to proceed 

Sucrose-utilizing transglucosidases are produced by bacteria belonging to various genera Leuconostoc, Lactobacillus, Weissella, Streptococcus, Deinococcus, Neisseria, Alteromonas, Pseudomonas, and Bifidobacterium (Table 2). 

Organism Enzyme Size (aa) Osidic linkage specificity References 

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