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Class III alcohol dehydrogenase: consistent pattern complemented with the mushroom enzyme
Author(s) -
Norin Annika,
Shafqat Jawed,
El-Ahmad Mustafa,
Alvelius Gunvor,
Cederlund Ella,
Hjelmqvist Lars,
Jörnvall Hans
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01524-2
Subject(s) - isozyme , agaricus bisporus , alcohol dehydrogenase , mushroom , biochemistry , edible mushroom , enzyme , formaldehyde dehydrogenase , complementary dna , protein subunit , protein primary structure , agaricus , biology , alcohol oxidase , chemistry , peptide sequence , stereochemistry , gene , glutathione , botany , recombinant dna , pichia pastoris
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.