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

Annika Norin; Jawed Shafqat; Mustafa El-Ahmad; Gunvor Alvelius; Ella Cederlund; Lars Hjelmqvist; Hans Jörnvall

doi:10.1016/s0014-5793(03)01524-2

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

Annika Norin·Jawed Shafqat·Mustafa El-Ahmad·Gunvor Alvelius·Ella Cederlund·Lars Hjelmqvist·Hans Jörnvall

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Abstract

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.

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Agaricus Aldehyde Oxidoreductases Base Sequence Binding Sites Evolution, Molecular Fungal Proteins Isoenzymes Models, Molecular Molecular Sequence Data Protein Subunits Sequence Analysis, DNA Structural Homology, Protein Journal Article Research Support, Non-U.S. Gov't

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Annika Norin, Jawed Shafqat, Mustafa El-Ahmad, Gunvor Alvelius, Ella Cederlund, Lars Hjelmqvist, Hans Jörnvall. 2004-02-13. Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme.. https://doi.org/10.1016/s0014-5793(03)01524-2

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