Citrate synthase from the thermophilic archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius

FEBS Letters

Hough, David W.¹  Stevenson, Kenneth J.²  Smith, Leon D.¹  Danson, Michael J.¹ 

[1] Department of Biochemistry, University of Bath, Bath BA2 7 AY, England;Division of Biochemistry, Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada

关键词: Citrate synthase;    Archaebacteria;    (Thermoplasma;    Sulfolobus);   

DOI  :  10.1016/0014-5793(87)81174-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Citrate synthase has been purified to homogeneity from the thermophilic archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius. From the relative molecular masses of the native proteins (85 and 83 kDa, respectively) and of their polypeptide chains (43 and 41 kDa, respectively) it is established that they are dimeric enzymes. The N-terminal sequence of the Thermoplasma citrate synthase was determined to be P-E-T-E-E-I-S-K-G-L-E-D-V-N-I-K. These properties are compared with those of citrate synthases from eubacteria and eukaryotes to extend the pattern of structural and functional diversity previously observed for this enzyme in non-archaebacterial species.

【 授权许可】

Unknown