Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114.

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.

journal_name

Appl Environ Microbiol

authors

Martínez-Rodríguez S,Las Heras-Vázquez FJ,Mingorance-Cazorla L,Clemente-Jiménez JM,Rodríguez-Vico F

doi

10.1128/aem.70.1.625-630.2004

keywords:

subject

Has Abstract

pub_date

2004-01-01 00:00:00

pages

625-30

issue

1

eissn

0099-2240

issn

1098-5336

journal_volume

70

pub_type

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