PMID:12455612
| Citation |
Cottrill, MA, Golovan, SP, Phillips, JP and Forsberg, CW (2002) Inositol phosphatase activity of the Escherichia coli agp-encoded acid glucose-1-phosphatase. Can. J. Microbiol. 48:801-9 |
|---|---|
| Abstract |
When screening an Escherichia coli gene library for myo-inositol hexakisphosphate (InsP6) phosphatases (phytases), we discovered that the agp-encoded acid glucose-1-phosphatase also possesses this activity. Purified Agp hydrolyzes glucose-1-phosphate, p-nitrophenyl phosphate, and InsP6 with pH optima, 6.5, 3.5, and 4.5, respectively, and was stable when incubated at pH values ranging from 3 to 10. Glucose-1-phosphate was hydrolyzed most efficiently at 55 degrees C. while InsP6 and p-nitrophenyl phosphate were hydrolyzed maximally at 60 degrees C. The Agp exhibited Km values of (0.39 mM, 13 mM, and 0.54 mM for the hydrolysis of glucose-1-phosphate, p-nitrophenyl phosphate, and InsP6, respectively. High-pressure liquid chromatography (HPLC) analysis of inositol phosphate hydrolysis products of Agp demonstrated that the enzyme catalyzes the hydrolysis of phosphate from each of InsP6, D-Ins(1,2,3,4,5)P5, Ins(1,3,4,5,6)P5, and Ins(1,2,3,4,6)P5, producing D/L-Ins(1,2,4,5,6)P5. D-Ins(1,2,4,5)P4, D/L-Ins(1,4,5,6)P4 and D/L-Ins(1,2,4,6)P4, respectively. These data support the contention that Agp is a 3-phosphatase. |
| Links | |
| Keywords |
Chromatography, High Pressure Liquid; Escherichia coli/enzymology; Escherichia coli/growth & development; Escherichia coli/immunology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Hydrolysis; Inositol Phosphates/metabolism; Kinetics; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/isolation & purification; Phosphoric Monoester Hydrolases/metabolism; Substrate Specificity |
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