Purification and characterization of the acetate forming enzyme, acetyl-CoA synthetase (ADP-forming) from the amitochondriate protist, Giardia lamblia.
Giardia lamblia, an amitochondriate eukaryote, contains acetyl-CoA synthetase (ADP-forming), an enzyme known only from one other eukaryote (Entamoeba histolytica) and a few anaerobic prokaryotes. The enzyme has been purified about 350-fold. The activity in the direction of acetate formation was dependent on ADP and inorganic phosphate. The reverse reaction could not be detected. Succinyl-CoA, propionyl-CoA and dADP were utilized with lower efficiency. The enzyme did not utilize AMP plus PPi thus differs from the broadly distributed acetyl-CoA synthetase (AMP-forming). The enzyme is responsible for acetate production accompanied by ATP generation, thus plays an important role in G. lamblia metabolism.
Sanchez
L B
LB
Rockefeller University, New York, NY 10021, USA.
Müller
M
M
D000106:Acetate-CoA Ligase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D000085:Acetates / Q000378:metabolism; D000105:Acetyl Coenzyme A / Q000378:metabolism; D000214:Acyl Coenzyme A / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000096:biosynthesis* / Q000378:metabolism; D000818:Animals; D003065:Coenzyme A / Q000378:metabolism; D016829:Giardia lamblia / Q000201:enzymology* / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D013379:Substrate Specificity
D000085:Acetates; D000214:Acyl Coenzyme A; D010710:Phosphates; C009061:propionyl-coenzyme A; D000244:Adenosine Diphosphate; D000105:Acetyl Coenzyme A; C012046:succinyl-coenzyme A; D000106:Acetate-CoA Ligase; D008274:Magnesium; D003065:Coenzyme A