Open AccessNucleotide sequence of the glyceraldehyde‐3‐phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum
Author(s) -
FABRY Stefan,
LANG Jutta,
Niermann Thomas,
Vingron Martin,
HENSEL Reinhard
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14568.x
Subject(s) - methanobacterium , thermophile , biochemistry , methanococcus , dehydrogenase , biology , peptide sequence , mesophile , sequence analysis , amino acid , nucleic acid sequence , enzyme , gene , genetics , bacteria , archaea
The genes for glyceraldehyde‐3‐phosphate dehydrogenase ( gap genes) from the mesophilic methanogenic archaebacteria Methanobacterium formicicum and Methanobacterium bryantii were cloned and sequenced. The deduced amino acid sequences show 95% identity to each other and about 70% identity to the glyceraldehyde‐3‐phosphate dehydrogenase from the thermophilic methanogenic archaebacterium Methanothermus fervidus . Although the sequence similarity between the archaebacterial glyceraldehyde‐3‐phosphate dehydrogenase and the homologous enzyme of eubacteria and eukaryotes is low, an equivalent secondary‐structural arrangement can be deduced from the profiles of the physical parameters hydropathy, chain flexibility and amphipathy. In order to find possible thermophile‐specific structural features of the enzyme from M. fervidus , a comparative primary‐sequence analysis was performed. Amino acid exchanges leading, to a stabilization of the main‐chain conformation, could be found throughout the sequence of the thermophile enzyme. Striking features of the thermophile sequence are the preference for isoleucine, especially in β‐sheets, and a low arginine/lysine ratio of 0.54.