The aconitase of yeast.  II. Crystallization and general properties of yeast aconitase.
Yeast aconitase [citrate (isocitrate) hydro-lyase, ED 4.2.1.3], inductively formed by Candida iipolytica in the presence of fluoroacetate, was purified approximately 100-fold by Sephadex G-100 gel filtration and DEAE-Sephadex column chromatography, yielding dark-brown needle crystals.  The crystalline aconitase was homogenious as judged by polyacrylamide gel electrophoresis and sedimentation by ultracentrifugation.  The enzyme showed maximal activity at pH 8.0 and at 55 degrees.  It has an S20, W of 5.03 S, a molecular weight of 68,500 and an isolectric point of pH 4.2.  The presence of 2.10 moles of iron per mole of the enzyme was demonstrated by atomic absorption spectroscopy.
D000154:Aconitate Hydratase / Q000302:isolation & purification / Q000378:metabolism; D002175:Candida / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004589:Electrophoresis, Disc; D006836:Hydro-Lyases; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000032:analysis; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D014461:Ultracentrifugation
D007501:Iron; D006836:Hydro-Lyases; D000154:Aconitate Hydratase