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Título

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

AutorSánchez-Moreno, Israel ; Iturrate Montoya, Laura; Martín-Hoyos, Rocio; Jimeno, M. Luisa ; Mena, Montaña; Bastida, Agatha; García-Junceda, Eduardo
Palabras claveBiotransformations
Catalytic promiscuity
Cofactors
Enzyme evolution
Metalloenzymes
Fecha de publicación22-oct-2009
SerieChembiochem. 2009 Jan 26;10(2):225-9.
ResumenEvolution 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 -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.
Descripción“This is the pre-peer reviewed version of the following article: Sánchez-Moreno, I., Iturrate, L., Martín-Hoyos, R., Jimeno, M. L., Mena, M., Bastida, A. and García-Junceda, E. (2009) From Kinase to Cyclase: An Unusual Example of Catalytic Promiscuity Modulated by Metal Switching. ChemBioChem. 10, 225-229, which has been published in final form at http://www3.interscience.wiley.com/journal/121544668/abstract?CRETRY=1&SRETRY=0.”
Versión del editorhttp://dx.doi.org/10.1002/cbic.200800573
URIhttp://hdl.handle.net/10261/17943
DOIDOI:10.1002/cbic.200800573
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