Reeve J N, Beckler G S
Department of Microbiology, Ohio State University, Columbus 43210.
FEMS Microbiol Rev. 1990 Dec;7(3-4):419-24. doi: 10.1111/j.1574-6968.1990.tb04947.x.
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.
迄今为止，所有在一级序列水平上研究过的原核（镍铁）氢化酶似乎都由一个共同的祖先序列进化而来。高度保守的半胱氨酰和组氨酰残基表明这些区域可能对酶活性、配体和辅因子结合至关重要。在几种不同的嗜热自养甲烷杆菌菌株中，编码甲基紫精氢化酶的基因上游基因间区域内有一段长度超过100个碱基对（bp）的高度保守序列，这表明需要这样长度的序列来指导和调节这些基因的表达。
