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Isocitrate Lyase Positive Serine Pathway 의 Key Enzyme 으로서의 Isocitrate Lyase
김현미,김유삼 ( Hyun Mi Kim,Yu Sam Kim ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.4
Isocitrate lyase as a key enzyme of isocitrate lyase positive serine pathway was purified by the combination of DEAE-Sephacel ion exchange chromatography and Sephadex G-150 gel filtration chromatography from Pseudomonas MA grown on methylamine as a sole carbon and nitrogen source. Molecular size of the enzyme was determined to be 158,000 dalton composed of four subunits, two 40,000 and two 38,000 dalton. Optimal pH for the enzyme was 7.6. Km and Vmax were 0.2 mM and 80 μmoles/min/㎎ protein, respectively. Anions, such as SO₄^(2-), NO₃^-, HPO₄^(2-), Cl^-, and CH₃COO^- were competitive inhibitors for the enzyme activity. Succinate and its analogs, malonate and itaconate, were noncompetitive inhibitors, whereas glyoxylate and oxalate were competitive inhibitors. 3-Bromopyruvate was a strong inhibitor, indicating that sulfhydryl group is localized on or near the active site of this enzyme. Phosphoenolpyruvate known as a regulatory molecule of anaplerotic glyoxylate cycle was also a noncompetitive inhibitor for this enzyme. It suggests that phosphoenolpyruvate may play regulatory role for the induced isocitrate lyase positive serine pathway.
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