Purification and properties of NAD(P)-independent polyol dehydrogenase complex from the plasma membrane of Gluconobacter oxydans.
Gluconobacter oxydans rapidly oxidizes many different polyhydroxy alcohols (polyols). Polyol oxidations are catalyzed by constitutively synthesized membrane-bound dehydrogenases directly linked to the electron transport chain. A polyol-oxidizing enzyme was isolated from the membranes of G. oxydans and tested for its ability to oxidize various substrates. The enzyme was composed of three subunits: a 67 kDa catalytic unit, a 46 kDa c-type cytochrome, and a 15 kDa subunit. The enzyme oxidized compounds containing three or more hydroxyl groups but did not oxidize mono-, di-, or cyclic alcohols; aldehydes; carboxylic acids; or mono- or di-saccharides. Therefore, we propose this enzyme be considered a polyol dehydrogenase.
VanLare
Ian J
IJ
Biology Department, Virginia Polytechnic Institute and State University, Blacksburg, VA 20460, USA. ivanlare@tusculum.edu
Claus
G W
GW
D002462:Cell Membrane / Q000201:enzymology*; D020600:Gluconobacter oxydans / Q000201:enzymology* / Q000648:ultrastructure; D007064:L-Iditol 2-Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013053:Spectrophotometry; D013379:Substrate Specificity
D007064:L-Iditol 2-Dehydrogenase