Catalytic Properties of Phosphoglucomutase from Pea Chloroplasts

L. V. Matasova and T. N. Popova^*

Department of Plant Physiology and Biochemistry, Voronezh State University, Universitetskaya pl. 1, Voronezh, 394693 Russia; E-mail: root@bc.vsu.ru

^* To whom correspondence should be addressed.

Received July 27, 1998; Revision received March 3, 1999

---

Electrophoretically homogeneous phosphoglucomutase (PGM) with specific activity of 3.6 units/mg protein was isolated from pea (Pisum sativum L.) chloroplasts. The molecular mass of this PGM determined by gel-filtration is 125 ± 4 kD. According to SDS-PAGE, the molecular mass of subunits is 65 ± 3 kD. The K_m for glucose-1-phosphate is 18.0 ± 0.5 µM, and for glucose-1,6-diphosphate it is 33 ± 0.7 µM. At glucose-1-phosphate and glucose-1,6-diphosphate concentrations above 0.5 and 0.2 mM, respectively, substrate inhibition is observed. The enzyme has optimum activity at pH 7.9 and 35°C. Mg²⁺ activates the PGM. Mn²⁺ activates the enzyme at concentrations below 0.2 mM, while higher concentrations have an inhibitory effect. The activity of the PGM is affected by 6-phosphogluconate, fructose-6-phosphate, NAD⁺, ATP, ADP, citrate, and isocitrate.

---

KEY WORDS: phosphoglucomutase, pea chloroplasts

---