Characterization of acetohydroxy acid synthase activity in the archaeon Haloferax volcanii.
Whereas the biochemistry of acetohydroxy acid synthase has been extensively studied in bacteria and eukaryotes, relatively little is known about the enzyme in archaea, the third kingdom of life. The present study biochemically characterizes acetohydroxy acid synthase activity in the halophilic archaea Haloferax volcanii. In addressing ion requirements, enzyme inhibition and antibody labeling, the results reveal that, except for its elevated salt requirements, the haloarchaeal enzyme is remarkably similar to its bacterial counterpart.
Vyazmensky
M
M
Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Barak
Z
Z
Chipman
D M
DM
Eichler
J
J
D000095:Acetolactate Synthase / Q000737:chemistry / Q000378:metabolism*; D000597:Amino Acids, Branched-Chain / Q000378:metabolism; D015153:Blotting, Western; D002413:Cations, Divalent / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D019622:Haloferax volcanii / Q000187:drug effects / Q000201:enzymology*; D007700:Kinetics; D011189:Potassium Chloride / Q000378:metabolism
D000597:Amino Acids, Branched-Chain; D002413:Cations, Divalent; D004791:Enzyme Inhibitors; D011189:Potassium Chloride; D000095:Acetolactate Synthase