Sugar synthesis in Leptospira. II. Presence of glyoxylate cycle enzymes.
The presence and some properties of the key enzymes of the glyoxylate cycle, isocitrate lyase (threo-Ds-isocitrate glyoxylate-lyase, EC 4.1.3.1) and malate synthase (L-malate glyoxylate-lyase (CoA-acetylating) EC 4.1.3.2), were investigated in Leptospira biflexa. Isocitrate lyase activity was found for the first time in the organism. The enzyme was induced by ethanol but not by acetate. The optimum pH was 6.8. The activity was inhibited by phosphoenolpyruvate, a specific inhibitor of isocitrate lyase. The optimum pH of malate synthase of L. biflexa was about 8.5. The Km value for glyoxylate was 3.0 X 10(-3) M and the activity was inhibited by glycolate, the inhibitor. The results strongly suggested the presence of a glyoxylate cycle in Leptospira. The possibility that the glyoxylate cycle plays an essential role in the synthesis of sugars, amino acids and other cellular components as an anaplerotic pathway of the tricarboxylic acid cycle in Leptospira was discussed.
D002241:Carbohydrates / Q000096:biosynthesis*; D006038:Glyoxylates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007522:Isocitrate Lyase / Q000378:metabolism*; D007919:Leptospira / Q000378:metabolism*; D008292:Malate Synthase / Q000378:metabolism*; D007652:Oxo-Acid-Lyases / Q000378:metabolism*
D002241:Carbohydrates; D006038:Glyoxylates; D008292:Malate Synthase; D007652:Oxo-Acid-Lyases; D007522:Isocitrate Lyase