Characteristics and sequence of phosphoglycolate phosphatase from a eukaryotic green alga Chlamydomonas reinhardtii
Phosphoglycolate phosphatase (PGPase), a key enzyme of photorespiration in
photosynthetic organisms, was purified from Chlamydomonas reinhardtii. The enzyme was
an∼ 65-kDa homodimer with a pI value of 5.1 composed of∼ 32-kDa subunits not
connected by any S–S bridges. It was also highly specific for phosphoglycolate with a K m
value of 140 μm and an optimal pH between 8 and 9. The activity was strongly inhibited by
CaCl 2, and it recovered competitively following the addition of MgCl 2 or EGTA. A mobility …
photosynthetic organisms, was purified from Chlamydomonas reinhardtii. The enzyme was
an∼ 65-kDa homodimer with a pI value of 5.1 composed of∼ 32-kDa subunits not
connected by any S–S bridges. It was also highly specific for phosphoglycolate with a K m
value of 140 μm and an optimal pH between 8 and 9. The activity was strongly inhibited by
CaCl 2, and it recovered competitively following the addition of MgCl 2 or EGTA. A mobility …