作者: Stefan FABRY , Jutta LANG , Thomas Niermann , Martin Vingron , Reinhard HENSEL
DOI: 10.1111/J.1432-1033.1989.TB14568.X
关键词: Methanobacteriales 、 Biology 、 Dehydrogenase 、 Amino acid 、 Isoleucine 、 Methanothermus fervidus 、 Sequence alignment 、 Biochemistry 、 Genetics 、 Nucleic acid sequence 、 Thermophile
摘要: The genes for glyceraldehyde-3-phosphate dehydrogenase (gap genes) from the mesophilic methanogenic archaebacteria Methanobacterium formicicum and bryantii were cloned sequenced. deduced amino acid sequences show 95% identity to each other about 70% thermophilic archaebacterium Methanothermus fervidus. Although sequence similarity between archaebacterial homologous enzyme of eubacteria eukaryotes is low, an equivalent secondary-structural arrangement can be profiles physical parameters hydropathy, chain flexibility amphipathy. In order find possible thermophile-specific structural features M. fervidus, a comparative primary-sequence analysis was performed. Amino exchanges leading, stabilization main-chain conformation, could found throughout thermophile enzyme. Striking are preference isoleucine, especially in β-sheets, low arginine/lysine ratio 0.54.