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拟南芥单结构域硫代硫酸盐硫转移酶的鉴定与表征

Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana.

作者信息

Bauer Michael, Papenbrock Jutta

机构信息

Institute for Botany, University of Hannover, Herrenhäuserstr. 2, D-30419, Hannover, Germany.

出版信息

FEBS Lett. 2002 Dec 18;532(3):427-31. doi: 10.1016/s0014-5793(02)03723-7.

Abstract

Sulfurtransferases/rhodaneses (ST) are a group of enzymes widely distributed in all three phyla that catalyze the transfer of sulfur from a donor to a thiophilic acceptor substrate. All ST contain distinct structural domains, and can exist as single-domain proteins, as tandemly repeated modules in which the C-terminal domain bears the active site, or as members of multi-domain proteins. We identified several ST in Arabidopsis resembling the C-terminus of the Arabidopsis two-domain ST1 and the single-domain GlpE protein from Escherichia coli. Two of them (accession numbers BAB10422 and BAB10409) were expressed in E. coli and purified. Both proteins showed thiosulfate-specific ST enzyme activity.

摘要

硫转移酶/硫氰酸酶(ST)是一类广泛分布于所有三个生物门类中的酶,它们催化硫从供体转移至亲硫受体底物。所有ST均含有独特的结构域,并且可以作为单结构域蛋白存在,作为C端结构域带有活性位点的串联重复模块存在,或者作为多结构域蛋白的成员存在。我们在拟南芥中鉴定出了几种类似于拟南芥双结构域ST1的C端以及来自大肠杆菌的单结构域GlpE蛋白的ST。其中两种(登录号分别为BAB10422和BAB10409)在大肠杆菌中表达并纯化。这两种蛋白均表现出硫代硫酸盐特异性ST酶活性。

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