Molecular Cloning, Purification, and Biochemical Characterization of Hydantoin Racemase from the Legume Symbiont Sinorhizobium meliloti CECT 4114-Reference-Cited by-同舟云学术

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

Published:2004-01 Issue:1 Volume:70 Page:625-630
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Martínez-Rodríguez Sergio¹,Las Heras-Vázquez Francisco Javier¹,Mingorance-Cazorla Lydia¹,Clemente-Jiménez Josefa María¹,Rodríguez-Vico Felipe¹

Affiliation:

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

Abstract

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/AEM.70.1.625-630.2004

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