EC Number   |
General Information |
Reference |
|---|
    2.6.1.45 | physiological function |
rice leaves usually show 3-4 times higher abundance of glutamate relative to serine, implicating that glutamate:glyoxylate aminotransferase GGAT may preferentially utilize glyoxylate to form glycine over serine:glyoxylate aminotransferase SGAT. When SGAT or GGAT activity is regulated by gene transformation or nitrogen deficiency, respectively, the glycine content is positively related to GGAT activities, while both serine and glycine contents are negatively related to SGAT activities, suggesting that GGAT preferentially catalyzes the conversion of glyoxylate into glycine while SGAT is mainly responsible for the transamination reaction of serine to hydroxypyruvate in the photorespiratory pathway of rice |
738913 |
| 2.6.1.45 | physiological function |
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation |
758661 |
| 2.6.1.45 | physiological function |
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation |
-, 758661 |
| 2.6.1.45 | physiological function |
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate |
759565 |
| 2.6.1.45 | physiological function |
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview |
-, 759565 |
