Phosphoglycolate phosphatase
Phosphoglycolate phosphatase(EC 3.1.3.18; systematic name 2-phosphoglycolate phosphohydrolase), also commonly referred to as phosphoglycolate hydrolase, 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for catalyzing the conversion of 2-phosphoglycolate into glycolate and phosphate: 2-phosphoglycolate + H2O = glycolate + phosphate First studied and purified within plants, phosphoglycolate phosphatase plays a major role in photorespiratory 2-phosphoglycolate metabolism, an essential pathway for photosynthesis in plants. The occurrence of photorespiration in plants, due to the lack of substrate specificity of rubisco, leads to the formation of 2-phosphoglycolate and 3-phosphoglycerate. 3-phosphogylcerate is the normal product of carboxylation and will enter the Calvin cycle. Phosphoglycolate, which is a potent inhibitor of phosphofructokinase and triosephosphate isomerase, must be quickly metabolized and transformed into a useful substrate, and phosphoglycolate phosphatase catalyzes the first step in the regeneration of 3-phosphoglycerate from 2-phosphoglycolate at the expense of energy in the form of ATP. Since the discovery of its activity in plants, it has been purified within human cells and implicated in 2,3-DPG regulation. Structure The structural characterization of phosphoglycolate phosphatase from Thermoplasma acidophilum (PDB 1L6R, pictured) revealed the monomer of the dimeric enzyme (indicated by the light blue and green coloring) includes two distinct domains, a smaller