CONSERVATION OF PRIMARY STRUCTURE IN PROKARYOTIC HYDROGENASES

被引：39

作者：

REEVE, JN

BECKLER, GS

机构：

[1] Department of Microbiology, The Ohio State University, Columbus, OH

来源：

FEMS MICROBIOLOGY LETTERS | 1990年 / 87卷 / 3-4期

关键词：

NICKEL BINDING; METHANOBACTERIUM-THERMOAUTOTROPHICUM; ARCHAEBACTERIA; METHANOGEN; GENE EVOLUTION; METHYL VIOLOGEN-REDUCING HYDROGENASE;

D O I：

10.1016/0378-1097(90)90489-D

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 of 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.

引用

页码：419 / 424

页数：6

共 37 条

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