Serine:glyoxylate aminotransferases from maize and wheat leaves: purification and properties.
Photorespiratory enzyme serine:glyoxylate aminotransferase (SGAT, EC 2.6.1.45) was purified from green parts of seedlings of two Gramminae species with different photosynthetic pathways, maize (Zea mays L., C(4) species) and wheat (Triticum aestivum L., C(3) species). The preparation from wheat was homogeneous as judged by SDS-PAGE with silver staining for proteins; however, the same method revealed approximately 9% contamination in a highly purified maize preparation. Molecular masses of SGAT from maize and wheat were estimated by SDS-PAGE to be 44.1 and 44.6 kDa, respectively. C(4) enzyme exhibited a specific activity in homogenates that was seven times lower than wheat, and this was associated with lower K (m) values for all substrates examined as well as a more than two times lower turnover number k (cat) with serine and glyoxylate as a pair of substrates. In contrast, the ratio of the turnover number to K (m)(Ser)(k (cat)/K (m)(Ser)) for C(4) aminotransferase proved to be about two times higher than for C(3) aminotransferase. The sensitivity of two enzymes to some inhibitors, especially aminooxyacetate, was different and they also differed with respect to thermal stability and pH optimum - the maize enzyme required 0.6 unit higher pH (8.6) for maximal activity and was more heat-resistant.
Truszkiewicz
Wiesław
W
Department of Biochemistry, Warsaw Agricultural University, Nowoursynowska 159, 02-776, Warsaw, Poland, paszkowski@delta.sggw.waw.pl.
Paszkowski
Andrzej
A