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Wiley, ChemBioChem, 2(10), p. 225-229, 2009

DOI: 10.1002/cbic.200800573

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From Kinase to Cyclase: An Unusual Example of Catalytic Promiscuity Modulated by Metal Switching

Journal article published in 2009 by Israel Sánchez-Moreno, Laura Iturrate, Rocio Martín-Hoyos, María Luisa Jimeno ORCID, Montaña Mena, Agatha Bastida ORCID, Eduardo García-Junceda
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This paper is available in a repository.

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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.