Reevaluation of citrate lyase from Escherichia coli.
The subunit structure of citrate lyase from Escherichia coli was shown to be similar to that of all other lyases investigated so far. The three different subunits with molecular masses of 55.5 kDa, (large subunit) 35 kDa (medium-sized subunit) and 12.5 kDa (small subunit, acyl carrier protein) occurred in a ratio of 1:1:1. Using high-pressure liquid chromatography, it was possible to demonstrate that the reported large acyl carrier protein, with a molecular mass of 85 kDa was a contaminating protein associated with citrate lyase multienzyme complex; it could be removed by anion-exchange chromatography with Q-Sepharose. The typical two configurations of citrate lyase, the 'star' form and the 'ring' form with a diameter of 14.3 nm and 15.4 nm, respectively, could be detected by electron microscopy.
D001426:Bacterial Proteins / Q000302:isolation & purification*; D004926:Escherichia coli / Q000201:enzymology*; D008854:Microscopy, Electron; D009097:Multienzyme Complexes / Q000302:isolation & purification*; D007652:Oxo-Acid-Lyases / Q000302:isolation & purification*; D011487:Protein Conformation
D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D007652:Oxo-Acid-Lyases; C019909:citrate (pro-3S)-lyase