Molecular and catalytic properties of 2,4-diacetylphloroglucinol hydrolase (PhlG) from Pseudomonas sp. YGJ3.

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.