In vitro phosphorylation of purified tobacco‐leaf phosphoenolpyruvate carboxylase

• Published in: FEBS letters Vol. 328; no. 1-2; pp. 215 - 218
• Main Authors: Wang, Yue-Hao, Chollet, Raymond
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 09.08.1993
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; C3 plant; CAM, Crassulacean acid metabolism; Chromatography, Gel; Chromatography, High Pressure Liquid; DTT, dithiothreitol; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; FPLC, fast-protein liquid chromatography; Fundamental and applied biological sciences. Psychology; In Vitro Techniques; Lyases; Molecular Sequence Data; MOPS, 3-(N-morpholino)propanesulfonic acid; Nicotiana - enzymology; PEG, polyethylene glycol; PEP, phosphoenolpyruvate; PEPC, phosphoenolpyruvate carboxylase; Phosphoenolpyruvate Carboxykinase (GTP) - metabolism; Phosphoenolpyruvate carboxylase; Phosphoenolpyruvate Carboxylase - isolation & purification; Phosphoenolpyruvate Carboxylase - metabolism; Phosphorylation; PK, protein kinase; Plants, Toxic; PMSF, phenylmethylsulfonyl fluoride; Protein kinase; Protein phosphorylation; Tobacco (Nicotiana tabacum L.); Zea mays - enzymology; Phosphorylation; Enzyme; Protein kinase; Dicotyledones; Angiospermae; Spermatophyta; Plant leaf; Solanaceae; Nicotiana tabacum; C3-Type; Phosphoenolpyruvate carboxylase

C3‐leaf phosphoenolpyruvate (PEP) carboxylase (PEPC) was purified about 1,000‐fold from tobacco and displayed a final specific activity of 35 μmol/min/mg protein, an apparent K m (total PEP) of 95 mM (both at (pH 8.0, 30°C), and an I50(l‐malate) value of 0.14 mM at pH 7.3, 0.2 mM PEP. The rapid, 5‐s...