title: Conservation of primary structure in prokaryotic hydrogenases.
abstract: All prokaryotic (NiFe)-hydrogenases so far studied at the primary sequence level appear to have evolved from a common ancestral sequence. Highly conserved cysteinyl and histidinyl residues indicate regions likely to be essential for enzyme activity, ligand and co-factor binding. There is a very highly conserved sequence over 100 basepairs (bp) in length within the intergenic region upstream of the methyl-viologen hydrogenase encoding genes in several different strains of Methanobacterium thermoautotrophicum, indicating that a sequence of this length is needed to direct and regulate the expression of these genes.
authors: Department of Microbiology, Ohio State University, Columbus 43210.
authors: J N
authors: JN
authors: Reeve
authors: G S
authors: GS
authors: Beckler
mesh_terms: D001105:Archaea / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D004269:DNA, Bacterial / Q000737:chemistry; D019605:Euryarchaeota / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D006864:Hydrogenase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data
chemical_list: D004269:DNA, Bacterial; D006864:Hydrogenase