Reversible and Irreversible Inhibitions of Glutamic and Arginine Decarboxylase Activities of Escherichia coli by Gallic Acid and d-Catechin.

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概要

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• Gallic acid and d-catechin inhibitions of glutamic and arginine decarboxylases of Escherichia coli occur in both reversible and irreversible manners. Gallic acid competes with the substrate in glutamic decarboxylase and with pyridoxal phoshate in arginine decarboxylase, whereas the interactions of d-catechin in both enzymes are of non-competitive nature with respects to both substrates and pyridoxal phosphate. Gallic acid and d-catechin combine with glutamic decarboxylase protein at different sites.

• 公益社団法人日本薬学会の論文
• 1962-09-25

著者

• 朴 昌基

  Kotaro Institute for Physiological Chemistry of Crude Drugs

• 桑野 重昭

  Kotaro Institute for Physiological Chemistry of Crude Drugs

• 朴 昌基

  School Of Pharmacy Osaka University

関連論文

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• Competition of Berberine with Pyridoxal Phosphate in the Tryptophanase System of Escherichia coli
• Effect of Berberine on Tyrosine Decarboxylase Activity of Streptococcus faeclis
• The Effect of Phenazine Derivatives on the Respiration of Microorganisms.
• Reversible and Irreversible Inhibitions of Glutamic and Arginine Decarboxylase Activities of Escherichia coli by Gallic Acid and d-Catechin.

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