Competition of Berberine with Pyridoxal Phosphate in the Tryptophanase System of Escherichia coli

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概要

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• It was found that berberine inhibits the tryptophanase system of Escherichia coli by competing with the coenzyme, pyridoxal phosphate, when acetone-dried cells or partially purified cell-free extracts were used as the enzyme. The inhibition was also found to be of irreversible nature. A mechanism was proposed to account for both the competitive and irreversible nature of the inhibition. Some kinetic considerations were made on the proposed mechanism. The inhibition of tryptophanase by berberine in intact cells was stronger than that in acetone-dried cells and it was inferred that different mechanisms are functioning in the inhibitions of the two types of cells.

• 社団法人日本薬学会の論文
• 1960-06-25

著者

• 山内 和子

  Kotaro Institute for Physiological Chemistry of Crude Drugs

• 桑野 重昭

  Kotaro Institute for Physiological Chemistry of Crude Drugs

関連論文

• Failure of Berberine to Inhibit Pig Heart Glutamic-Aspartic Transaminase.
• Further Studies on Competition of Berberine with Pyridoxal Phosphate in the Tryptophanase System of Escherichia coli.
• Competition of Berberine with Pyridoxal Phosphate in the Tryptophanase System of Escherichia coli
• Effect of Berberine on Tyrosine Decarboxylase Activity of Streptococcus faeclis
• Reversible and Irreversible Inhibitions of Glutamic and Arginine Decarboxylase Activities of Escherichia coli by Gallic Acid and d-Catechin.

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