EC Number   |
Natural Substrates |
|---|
    4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
- |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
one of the enzymes involved in tetrahydrobiopterin biosynthesis |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
23 bp exon 3 skipping in transcription rather than post-transcriptional mechanisms is a major cause of the low PTPS protein expression in human macrophages and related cell types. The exon lacking leads to a premature stop codon encoding for a shorter protein instead of the full-length functional enzyme |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
rate-limiting enzyme in the synthesis of human tetrahydrobiopterin |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme catalyzes the first step in the conversion of 7,8-dihydroneopterin triphosphate to tetrahydrobiopterin |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme is involved in tetrahydrobiopterin biosynthesis |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme has six active sites located at the interface of three subunits. The enzyme contains an intersubunit catalytic triad motif composed of the amino acid residues Cys A42, His B89 and Asp B88 which is involved in the abstraction of protons from the substrate side-chain carbons. The gamma and beta phosphates of the substrate are essential for substrate binding and enhance the catalytic efficiency |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme is post-translationally phosphorylated in several Ser residues by protein kinases. The enzyme requires the phosphoserine 19 residue for maximal activity under in vivo conditions. Mutant enzymes with alterations in the protein kinase recognition site, phosphoserine 19 residue, are not phosphorylated by protein kinase and have reduced activity |
| 4.2.3.12 | 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin |
the enzyme catalyzes the second step of tetrahydrobiopterin (BH4) synthesis |
