CITRATE SYNTHASE FROM THE HYPERTHERMOPHILIC ARCHAEON, PYROCOCCUS-FURIOSUS

被引：41

作者：

MUIR, JM ^{[1
]}

RUSSELL, RJM ^{[1
]}

HOUGH, DW ^{[1
]}

DANSON, MJ ^{[1
]}

机构：

[1] UNIV BATH,SCH BIOL & BIOCHEM,BATH BA2 7AY,AVON,ENGLAND

来源：

PROTEIN ENGINEERING | 1995年 / 8卷 / 06期

基金：

英国生物技术与生命科学研究理事会;

关键词：

ARCHAEA; CITRATE SYNTHASE; HOMOLOGY MODELING; PYROCOCCUS; THERMOPHILES;

D O I：

10.1093/protein/8.6.583

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The gene encoding the enzyme citrate synthase has been cloned and sequenced from the hyperthermophilic Archaeon Pyrococcus furiosus, and the derived amino acid sequence has been phylogenetically compared with citrate synthases from archaeal, bacterial and eukaryal organisms. The gene has been over-expressed in Escherichia coli to produce an active enzyme that has then been characterized with respect to its kinetic, oligomeric and hyperthermostable properties. A structurally-based sequence alignment was made to the citrate synthase from the thermophilic Archaeon Thermoplasma acidophilum, the crystal structure of which we have determined recently. From this alignment, a homology-modelled structure for the P.furiosus citrate synthase was generated and analysed.

引用

页码：583 / 592

页数：10

共 31 条

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