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Drosophila alcohol dehydrogenase: evaluation of Ser 139 site‐directed mutants
Author(s) -
Cols Neus,
Atrian Sı́lvia,
Benach Jordi,
Ladenstein Rudolf,
Gonzàlez-Duarte Roser
Publication year - 1997
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(97)00894-6
Subject(s) - alcohol dehydrogenase , residue (chemistry) , chemistry , mutant , catalysis , catalytic triad , stereochemistry , triad (sociology) , enzyme , ethanol , alcohol , dehydrogenase , alcohol oxidoreductase , biochemistry , active site , nad+ kinase , psychology , psychoanalysis , gene
Drosophila alcohol dehydrogenase (DADH) belongs to the large and highly heterogeneous (15–30% residue identity) short‐chain dehydrogenase/reductase family (SDR). It is the only reported member that oxidizes mainly ethanol and 2‐propanol among other alcohols. To confirm the role of Ser 139 we constructed two site‐directed mutants, Ser 139 Ala and Ser 139 Cys, which show no enzymatic activity. Molecular replacement and data from crystallographically refined 3D structures confirm the position of Ser 139 , whose hydroxyl group faces the cleft of the presumed catalytic pocket, very close to Tyr 152 and Lys 156 . Thus, consistent with the constitution of the catalytic triad of other SDR, our results suggest that Ser 139 of DADH is directly involved in the catalytic reaction.