Abstract
Evolution of new enzyme functions: We describe the promiscuous behaviour of the dihydroxyacetone (DHA) kinase from Citrobacter freundii strain CECT 4626. In addition to the transfer of the γ-phosphate of adenosine-5′-triphosphate (ATP) to DHA, this ATP-dependent DHAK is able to catalyse the cyclization of FAD to yield riboflavin 4′,5′-cyclic phosphate (4′,5′-cFMN). This catalytic promiscuity is modulated by the divalent cation that forms the complex with the phosphorylated substrate.
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