Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114 |
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Authors: | Martínez-Rodríguez Sergio Las Heras-Vázquez Francisco Javier Mingorance-Cazorla Lydia Clemente-Jiménez Josefa María Rodríguez-Vico Felipe |
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Affiliation: | Departamento de Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, La Ca?ada de San Urbano, E-04120 Almería, Spain. |
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Abstract: | Hydantoin racemase from Sinorhizobium meliloti was functionally expressed in Escherichia coli. The native form of the enzyme was a homotetramer with a molecular mass of 100 kDa. The optimum temperature and pH for the enzyme were 40 degrees C and 8.5, respectively. The enzyme showed a slight preference for hydantoins with short rather than long aliphatic side chains or those with aromatic rings. Substrates, which showed no detectable activity toward the enzyme, were found to exhibit competitive inhibition. |
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