EC Number   |
General Information |
Reference |
|---|
   2.6.1.52 | evolution |
phosphoserine aminotransferases belong to the class IV of aminotransferases with the alpha-type fold. In general, this class of enzymes is characterized by the presence of two domains with mixed alpha/beta fold |
759284 |
| 2.6.1.52 | evolution |
the Arabidopsis genome contains three genes for the PGDH (At4g34200/PGDH1, At1g17745/ PGDH2, and At3g19480/ PGDH3), two genes for the PSAT (At4g35630/PSAT1, and At2g17630/PSAT2) and one gene for the PSP (At1g18640). The PSAT1 gene is the most expressed isoform in Arabidopsis thaliana |
759278 |
| 2.6.1.52 | malfunction |
a growth phenotype is observed for PSAT1-silenced plants due to serine deficiency |
759278 |
| 2.6.1.52 | malfunction |
a sericin-deficient silkworm strain exhibits a diminished expression of bmPSAT mRNA in the silk gland |
-, 758704 |
| 2.6.1.52 | malfunction |
deletion of 45 N-terminal residues (EhPSAT_DELTA45) results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein |
-, 759344 |
| 2.6.1.52 | metabolism |
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis |
759886 |
| 2.6.1.52 | metabolism |
L-serine is involved in several important metabolic pathways in the protozoan parasite Entamoeba histolytica. Phosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing L-serine |
-, 759344 |
| 2.6.1.52 | metabolism |
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. This pathway composed of D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95), PSAT, and phosphoserine phosphatase (PSP, EC 3.1.3.3) is crucial for the de novo production of L-serine from a glycolytic intermediate, 3-phosphoglycerate |
-, 758704 |
| 2.6.1.52 | metabolism |
phosphoserine aminotransferase (PSAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. This process in plants takes place in plastids. It is a part of the phosphorylated pathway of serine biosynthesis, one of three routes recognized in plant organisms that yield serine. In this three-step biotransformation, 3-phosphoglycerate (3-PGA) delivered from plastidial glycolysis and Calvin cycle is oxidized by 3-PGA dehydrogenase. Then, 3-PHP is subjected to transamination with Glu to yield PSer and 2-oxoglutarate (AKG). In the last step of the pathway, serine is produced by the action of phosphoserine phosphatase |
759284 |
| 2.6.1.52 | metabolism |
the serine biosynthesis pathway consists of three sequential reactions that are catalyzed by 3-phosphoglycerate dehydrogenase (PGDH), 3-phosphoserine aminotransferase (PSAT), and 3-phosphoserine phosphatase (PSP) enzymes, all localized in the plastids. Serine biosynthesis pathways in plants, overview |
759278 |
