title: Spinach chloroplast thioredoxins in evolutionary drift.
abstract: The amino acid sequences surrounding the active sites of spinach chloroplast thioredoxins m and f have been determined. Both types of thioredoxins share common ancestor genes with the E. coli one, demonstrated by invariant active site sequences. The m-type thioredoxins have closer homology with the E. coli one in the sequence analyzed as well as in enzymatic specificity, whereas the f-type is less homologous both in sequence and specificity. It suggests that the m-type gene represents a prototype conserved throughout evolutionary processes whereas the f-type has undergone mutations resulting in a modified specificity.
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001665:Binding Sites; D005075:Biological Evolution; D002736:Chloroplasts / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D007700:Kinetics; D009154:Mutation; D010944:Plants / Q000235:genetics*; D013045:Species Specificity; D013879:Thioredoxins / Q000235:genetics* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D013879:Thioredoxins