PRIMARY STRUCTURE OF A MULTIMERIC PROTEIN, HOMOLOGOUS TO THE PEP-UTILIZING ENZYME FAMILY AND ISOLATED FROM A HYPERTHERMOPHILIC ARCHAEBACTERIUM

被引：13

作者：

CICICOPOL, C ^{[1
]}

PETERS, J ^{[1
]}

KELLERMANN, J ^{[1
]}

BAUMEISTER, W ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,D-82152 MARTINSRIED,GERMANY

来源：

FEBS LETTERS | 1994年 / 356卷 / 2-3期

关键词：

PEP SYNTHASE; PEP-UTILIZING; ARCHAEA; HYPERTHERMOPHILIC;

D O I：

10.1016/0014-5793(94)01304-7

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：

A large protein complex (approx. 2000 kDa) was found in the cytosol of the hyperthermophilic archaebacterium Staphylothermus marinas. The purified protein was shown to be a homomultimer of 93 kDa subunits, the primary structure of which was determined by nucleotide sequence analysis. The protein belongs to the family of phosphoenolpyruvate-utilizing enzymes and represents the first member characterized in archaebacteria. Its homomultimeric organisation differs from the typically dimeric structure of its eubacterial and eukaryotic counterparts.

引用

页码：345 / 350

页数：6

共 16 条

[1] BASIC LOCAL ALIGNMENT SEARCH TOOL [J].