Article
Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis.
Biochimica et biophysica acta - 1 Feb 2006
Andújar-Sánchez Montserrat, Martínez-Rodríguez Sergio, Heras-Vázquez Francisco Javier Las, Clemente-Jiménez Josefa María, Rodríguez-Vico Felipe, Jara-Pérez Vicente
Abstract excerpt
Hydantoin racemase enzyme together with a stereoselective hydantoinase and a stereospecific d-carbamoylase guarantee the total conversion from d,l-5-monosubstituted hydantoins with a low velocity of racemization, to optically pure d-amino acids. Hydantoin racemase from Sinorhizobium meliloti was expressed in Escherichia coli. Calorimetric and fluorescence experiments were then carried out to obtain the...
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