Molecular and Catalytic Properties of 2,4-Diacetylphloroglucinol Hydrolase (PhlG) from Pseudomonas sp. YGJ3

Abstract

Gene phlG encoding 2,4-diacetylphloroglucinol hydrolase was cloned from Pseudomonas sp. YGJ3 and expressed in Escherichia coli. Recombinant PhlG was purified homogeneously. It required 2-mercaptoethanol for stability. K_m for 2,4-diacetylphloroglucinol and k_cat were determined to be 24 µM and 5.8 s⁻¹ respectively. CoCl₂ specifically and significantly activated PhlG.