Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme

FEBS Letters

Shafqat, Jawed¹  Norin, Annika¹  Hjelmqvist, Lars¹  El-Ahmad, Mustafa¹  Cederlund, Ella¹  Alvelius, Gunvor¹  Jörnvall, Hans¹ 

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden

关键词: Alcohol dehydrogenase class I and III;    Isozyme;    Pattern recognition;    Active site;    Mushroom enzyme;    ADH;    alcohol dehydrogenase;    MDR;    medium-chain dehydrogenase/reductase;   

DOI  :  10.1016/S0014-5793(03)01524-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mushroom alcohol dehydrogenase (ADH) from Agaricus bisporus (common mushroom, champignon) was purified to apparent homogeneity. One set of ADH isozymes was found, with specificity against formaldehyde/glutathione. It had two highly similar subunits arranged in a three-member isozyme set of dimers with indistinguishable activity. Determination of the primary structure by a combination of chemical, mass spectrometric and cDNA sequence analyses, correlated with molecular modeling towards human ADHs, showed that the active site residues are of class III ADH type, and that the subunit differences affect other residues. Class I and III forms of ADHs characterized define conserved substrate-binding residues (three and eight, respectively) useful for recognition of these enzymes in any organism.

【 授权许可】

Unknown