Review
doi: 10.1111/j.1574-6968.1990.tb04947.x.
Conservation of primary structure in prokaryotic hydrogenases
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- PMID: 2128802
- DOI: 10.1111/j.1574-6968.1990.tb04947.x
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Review
Conservation of primary structure in prokaryotic hydrogenases
FEMS Microbiol Rev.
1990 Dec.
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.
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