Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541.
The structure of the alcohol dehydrogenase ADH-'A' from Rhodococcus ruber reveals possible reasons for its remarkable tolerance to organic co-solvents and suggests new directions for structure-informed mutagenesis to produce enzymes of altered substrate specificity or improved selectivity.
Karabec
Martin
M
Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/3, A-8010 Graz, Austria.
Łyskowski
Andrzej
A
Tauber
Katharina C
KC
Steinkellner
Georg
G
Kroutil
Wolfgang
W
Grogan
Gideon
G
Gruber
Karl
K
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D000438:Alcohols / Q000138:chemical synthesis / Q000737:chemistry; D018360:Crystallography, X-Ray; D007659:Ketones / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D012240:Rhodococcus / Q000201:enzymology*; D012997:Solvents / Q000737:chemistry; D013379:Substrate Specificity
D000438:Alcohols; D007659:Ketones; D012997:Solvents; D000426:Alcohol Dehydrogenase