The distinctiveness of ATP:citrate lyase from Aspergillus nidulans.
ATP:citrate lyase (ACL), an important enzyme in lipid synthesis, has been purified from Aspergillus nidulans to a specific activity of 19.6 micromol min(-1) mg(-1), almost twice that of any other purified ACL and shown to be distinct from any previously purified ACL. The enzyme is a 371+/-31 kDa hexamer of 3 alpha, 3 beta proteins, unlike the 4 alpha tetramer found in rats or yeasts. The molecular weights of the alpha and beta protein subunits were determined by SDS-PAGE to be 70 and 55 kDa. ACL in A. nidulans (unlike Aspergillus niger) appears to be regulated by the carbon source present in the media. In crude extracts, it was found at high activity (88 micromol min(-1) mg protein(-1)) in glucose-grown cells but only at low activity (10 micromol min(-1) mg protein(-1)) in acetate-grown cells.
Adams
Ian P
IP
Department of Biological Sciences, University of Hull, Hull HU6 7RX, UK. I.P.Adams@Medschool.Hull.ac.uk
Dack
Stephen
S
Dickinson
F Mark
FM
Ratledge
Colin
C
D001275:ATP Citrate (pro-S)-Lyase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D001233:Aspergillus nidulans / Q000201:enzymology* / Q000254:growth & development; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose
D017886:Durapatite; D001275:ATP Citrate (pro-S)-Lyase; D005947:Glucose; D000645:Ammonium Sulfate