Extended superfamily of short alcohol‐polyol‐sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases

FEBS Letters

von Bahr-Lindström, Hedvig²  Fröschle, Marion¹  Jany, Klaus-Dieter¹  Jörnvall, Hans²  Ulmer, Wolfgang¹ 

[1] Institute for Organic Chemistry, Biochemistry and Isotope Research, Stuttgart University, D-7000 Stuttgart 80, FRG;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Homology;    Alignment;    Short dehydrogenase;    Superfamily;    Non-zinc alcohol dehydrogenase;   

DOI  :  10.1016/0014-5793(84)80167-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The recently determined primary structure of glucose dehydrogenase from Bacillus megaterium was scanned by computerized comparisons for similarities with known polyol and alcohol dehydrogenases. The results revealed a highly significant similarity between this glucose dehydrogenase and ribitol dehydrogenase from Klebsiella aerogenes. Sixty-one positions of the 262 in glucose dehydrogenase are identical between these two proteins (23% identity), fitting into a homology alignment for the complete polypeptide chains. The extent of similarity is equivalent to that between other highly divergent but clearly related dehydrogenases (two zinc-containing alcohol dehydrogenases, 25% sorbitol and zinc-containing alcohol dehydrogenases, 25%; ribitol and non-zinc-containing alcohol dehydrogenases, 20%), and suggests an ancestral relationship between glucose and ribitol dehydrogenases from different bactera. The similarities fit into a previously suggested evolutionary scheme comprising short and long alcohol and polyol dehydrogenases, and greatly extend the former group to one composed of non-zinc-containing alcohol-polyol-glucose dehydrogenases.

【 授权许可】

Unknown