Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation.
Sliwa
Dariusz A
DA
Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, USA.
Krishnakumar
Arathi M
AM
Peters
John W
JW
Ensign
Scott A
SA
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019943:Amino Acid Substitution; D001483:Base Sequence; D019295:Computational Biology; D017931:DNA Primers; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D020584:Xanthobacter / Q000201:enzymology*
D017931:DNA Primers; D004269:DNA, Bacterial; D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; C450599:2-hydroxypropylthioethanesulfonate dehydrogenase, Xanthobacter; D000426:Alcohol Dehydrogenase