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Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114
dc.contributor.author | Martínez Rodríguez, Sergio | |
dc.contributor.author | Las Heras Vázquez, Francisco Javier | |
dc.contributor.author | Mingorance Cazorla, Lidia | |
dc.contributor.author | Clemente Jiménez, Josefa María | |
dc.contributor.author | Rodríguez Vico, Felipe | |
dc.date.accessioned | 2024-05-22T12:48:21Z | |
dc.date.available | 2024-05-22T12:48:21Z | |
dc.date.issued | 2004 | |
dc.identifier.issn | 0099-2240 | |
dc.identifier.uri | http://hdl.handle.net/10835/16547 | |
dc.description.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°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. | es_ES |
dc.language.iso | en | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Hydantoin Racemase | es_ES |
dc.subject | Sinorhizobium meliloti | es_ES |
dc.subject | D,L-5-monosubstituted hydantoins | es_ES |
dc.subject | Molecular Cloning | es_ES |
dc.subject | Purification | es_ES |
dc.subject | Biochemical Characterization | es_ES |
dc.title | Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114 | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |