EC Number   |
General Information |
Reference |
|---|
   2.8.2.20 | evolution |
in humans, there are only two TPST isoforms, designated TPST1 and TPST2 |
762445 |
| 2.8.2.20 | evolution |
the catalytic domain of sulfotransferases is unrelated to that of protein kinases, and moreover, the way in which the substrates are held are different. Protein kinases have a deep cleft into which ATP binds and the protein substrate binds to the surface proximal to this cleft. ATP is held in an orientation that buries the adenine base. In contrast, the active site of sulfotransferase comprises a tunnel with the binding sites for PAPS and peptide/glycan substrate is at either end, PAPS binds to the active site of sulfotransferases in an orientation that exposes the adenine base to solvent |
760529 |
| 2.8.2.20 | malfunction |
Arabidopsis thaliana tpst mutants are hypersensitive to fructose. In contrast to sucrose and glucose, fructose represses primary root growth of various ecotypes of Arabidopsis at low concentrations. RNA-seq analysis identified 636 differentially expressed genes (DEGs) in Col-0 seedlings in response to fructose verses glucose. Fructose downregulates genes involved in photosynthesis, glucosinolate biosynthesis and IAA biosynthesis, but upregulates genes involved in the degradation of branched amino acids, sucrose starvation response, and dark response. The fructose upregulated DEGs include genes encoding two AtTPST substrate proteins, phytosulfokine-alpha (PSK-alpha) and root meristem growth factor 7 (RGF7). Synthesized peptides of PSK-alpha and RGF7 can restore the fructose hypersensitivity of tpst mutant plants. Auxin distribution and accumulation at the root tip are affected by fructose and the tpst mutation |
-, 762151 |
| 2.8.2.20 | malfunction |
deficiency in the enzymatic activity of isozyme TPST2 causes growth-retardation in mice, autosomal recessive hypothyroidism, and lifelong female infertility. The isozyme deficiency is also involved in severe thyroid hypogenesis and consequent dwarfism, due to the impairment of the tyrosine sulfation of thyroid-stimulating hormone receptor by mutant TPST2 |
705417 |
| 2.8.2.20 | malfunction |
knockdown of the enzyme blocks the cuticle localization of ROL-6 |
-, 725976 |
| 2.8.2.20 | malfunction |
mechanistic inhibition of cellular tyrosine sulfation might be relevant to some of the phenotypes observed in cells exposed to anionic TPST ligands and RAF protein kinase inhibitors. Multiple RAF kinase inhibitors target TPST catalytic activity in vitro |
760527 |
| 2.8.2.20 | malfunction |
mutation of the enzyme leads to defective maintenance of the root stem cell niche, decreased meristematic activity, and stunted root growth. Mutation of the enzyme also impairs basal- and auxin-induced expression of the Plethora stem cell transcription factor genes |
726161 |
| 2.8.2.20 | metabolism |
biological sulfation (also called sulfonation) is a widespread covalent chemical modification of biomolecules by the addition of a sulfonyl group (SO3-). Inorganic sulfate is made available for incorporation into biomolecules in the form of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) through a process in which ATP is first sulfated by the ATP sulfurylase enzyme to generate adenosine 5'-phosphosulfate, which is then phosphorylated on the 3' position of the ribose ring to generate PAPS. Sulfation is carried out by a class of enzymes called sulfotransferases |
760529 |
| 2.8.2.20 | metabolism |
the two independent TPSTs catalyze the tyrosine-O-sulfation, a post-translational modification |
703588 |
| 2.8.2.20 | more |
the cytoplasmic N-terminus and the transmembrane domain are not required for enzymatic activity |
761815 |
