Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114
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Martínez Rodríguez, Sergio; Las Heras Vázquez, Francisco Javier; Mingorance Cazorla, Lidia; Clemente Jiménez, Josefa María; Rodríguez Vico, FelipeDate
2004Abstract
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°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.
Palabra/s clave
Hydantoin Racemase
Sinorhizobium meliloti
D,L-5-monosubstituted hydantoins
Molecular Cloning
Purification
Biochemical Characterization