Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
Hurley
T D
TD
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202, USA. hurley@biochem6.iupui.edu
Steinmetz
C G
CG
Xie
P
P
Yang
Z N
ZN
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012984:Software
D007527:Isoenzymes; D011994:Recombinant Proteins; D000426:Alcohol Dehydrogenase