| Literature DB >> 14711700 |
Sergio Martínez-Rodríguez1, Francisco Javier Las Heras-Vázquez, Lydia Mingorance-Cazorla, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico.
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.Entities:
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Year: 2004 PMID: 14711700 PMCID: PMC321266 DOI: 10.1128/AEM.70.1.625-630.2004
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792