INHIBITION OF ACTIVITIES OF ASPARTATE AMINO-TRANSFERASE AND TRYPTOPHANASE BY EXCESS BINDING OF PYRIDOXAL 5'-PHOSPHATE

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概要

• 論文の詳細を見る

• Pyridoxal 5'-phosphate (PLP), in high concentrations, was found to bind to lysine residues at non-catalytic sites of mammalian aspartate aminotransferase (GOT) and E. coil tryptophanase. This excess bind-ing of PLP caused significant decreases in the activities of these enzymes. The concentrations of PLP required for the 50% inhibition of GOT and tryptophanase were 2.5mM and 6.3mM, respectively. Pyridoxal (PL) also combined with these enzymes by forming SCHIFF's bases with lysine residues at the catalytic as well as non-catalytic sites. The concentration of PL necessary for the 50% inhibition of GOT activity was 5mM, indicating that the inhibitory action of PL is lower than that of PLP.

• 財団法人 学会誌刊行センターの論文

著者

• 福井 三郎

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, K

• 清水 祥一

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University

• 真杉 文紀

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University

• 名取 与平

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University

• 福井 三郎

  Laboratory of Industrial Biochemistry, Deparmtnt of Industrial Chemistry, Faculty of Engineering, Kyoto University

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• INHIBITION OF ACTIVITIES OF ASPARTATE AMINO-TRANSFERASE AND TRYPTOPHANASE BY EXCESS BINDING OF PYRIDOXAL 5'-PHOSPHATE
• COENZYMATIC ACTIVITIES OF 2-NOR-2-HYDROXY-METHYL PYRIDOXAL 5'-PHOSPHATE FOR VARIOUS VITAMIN B6 ENZYMES
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• Spectrophotometric Demonstration of Vitamin B12S-Formation by Nucleophilic Cleavage of Co-C Bond of Acetylcobalamin
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