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Corn phosphoglycolate phosphatase: purification and properties.

P Hardy¹, P Baldy

¹Unité Associée au C.N.R.S. no 241, Centre de Physiologie Végétale de l'Université Paul Sabatier, F-31062, Toulouse, France.

|November 16, 2013

Summary

This study purified phosphoglycolate phosphatase from maize, revealing its optimal activity and requirement for Mg(2+). The enzyme

Area of Science:

Biochemistry
Plant Physiology
Enzymology

Background:

Phosphoglycolate phosphatase (PGP) plays a role in photorespiration.
Understanding PGP activity in maize bundle sheath chloroplasts is crucial for plant metabolism.

Purpose of the Study:

To purify and characterize phosphoglycolate phosphatase from maize leaf bundle sheath.
To investigate the kinetic properties and structural features of maize PGP.

Main Methods:

Enzyme purification using Sephadex G-75, DEAE-cellulose, and Phospho-Ultrogel A6R chromatography.
Enzyme activity assays, kinetic analysis (Michaelis-Menten kinetics), isoelectric focusing, and gel electrophoresis (native and SDS-PAGE).

Main Results:

200-fold purification of PGP with specific activity of 99 μmol mg(-1) protein·min(-1).

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Optimal activity between pH 6.3-8.0, high specificity for phosphoglycolate, and requirement for Mg(2+) (Km=0.015 mM).

Native molecular mass of ~61,500 Da and subunit molecular mass of ~31,500 Da, indicating a dimeric structure.

Conclusions:

Maize phosphoglycolate phosphatase is a dimer with specific kinetic properties.
Stromal pH and Mg(2+) variations during dark-light transitions may not directly regulate PGP activity in bundle-sheath chloroplasts.