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来自豆科植物共生菌苜蓿中华根瘤菌CECT 4114的乙内酰脲消旋酶的分子克隆、纯化及生化特性分析

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

作者信息

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

机构信息

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

出版信息

Appl Environ Microbiol. 2004 Jan;70(1):625-30. doi: 10.1128/AEM.70.1.625-630.2004.

DOI:10.1128/AEM.70.1.625-630.2004
PMID:14711700
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC321266/
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.

摘要

来自苜蓿中华根瘤菌的乙内酰脲消旋酶在大肠杆菌中实现了功能表达。该酶的天然形式是一种分子量为100 kDa的同四聚体。该酶的最适温度和pH分别为40℃和8.5。该酶对具有短脂肪族侧链而非长脂肪族侧链或带有芳香环的乙内酰脲表现出轻微偏好。对该酶无明显活性的底物被发现具有竞争性抑制作用。

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1
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本文引用的文献

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