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Applied and Environmental Microbiology, January 2004, p. 625-630, Vol. 70, No. 1
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.1.625-630.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114

Sergio Martínez-Rodríguez, Francisco Javier Las Heras-Vázquez, Lydia Mingorance-Cazorla, Josefa María Clemente-Jiménez, and Felipe Rodríguez-Vico*

Departamento de Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, La Cañada de San Urbano, E-04120 Almería, Spain

Received 19 June 2003/ Accepted 8 October 2003

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.

* Corresponding author. Mailing address: Departamento de Química-Física, Bioquímica y Química Inorgánica, Edificio C.I.T.E. I., Universidad de Almería, La Cañada de San Urbano, E-04120 Almería, Spain. Phone: 34-950-015055. Fax: 34-950-015008. E-mail: fvico{at}ual.es.

Applied and Environmental Microbiology, January 2004, p. 625-630, Vol. 70, No. 1
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.1.625-630.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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