Structure-function relationships in Drosophila melanogaster alcohol dehydrogenase allozymes ADH(S), ADH(F) and ADH(UF), and distantly related forms

European Journal of Biochemistry

Volumn 267, Issue 12, 2000, Pages 3613-3622

  Benach, Jordi ^a   Atrian, Sílvia ^a,b   Fibla, Joan ^c   Gonzàlez Duarte, Roser ^b   Ladenstein, Rudolf ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF BARCELONA   (Spain)

^c UNIVERSITY OF LLEIDA   (Spain)

Author keywords

3D model structure; Alcohol dehydrogenase; Drosophila melanogaster; Molecular evolution; Natural polymorphism

Indexed keywords

ALCOHOL DEHYDROGENASE; ALLOENZYME; INSECT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; DROSOPHILA MELANOGASTER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; MOLECULAR EVOLUTION; MOLECULAR MODEL; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; ANIMALS; ANTIBODIES, MONOCLONAL; CATALYTIC DOMAIN; DROSOPHILA MELANOGASTER; EPITOPE MAPPING; ISOENZYMES; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0033917432     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01390.x     Document Type: Article

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