PTS
PTS (6-pyruvoyltetrahydropterin synthase, also known as PTPS) is a lyase of the PTPS family that acts in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. It catalyses the second, irreversible step in the pathway from GTP. Browse Assay Genie's current range of PTS research reagents below, or read on for the biology behind the target.
PTS is an enzyme in the pathway that produces tetrahydrobiopterin (BH4) from GTP. It catalyses the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin, which it does by eliminating inorganic triphosphate from dihydroneopterin triphosphate. This is the second step of the pathway and it is irreversible, so the activity of PTS commits the intermediate to BH4 synthesis.
BH4 is an essential cofactor of the aromatic amino acid hydroxylases. It also acts as a regulator of various enzyme activities, including enzymes involved in serotonin biosynthesis and nitric oxide synthase activity. Through its role in making this cofactor, PTS therefore sits upstream of several distinct biochemical processes, which makes it a useful point of study in cofactor metabolism.
The human PTS gene encodes a protein of the PTPS family, classified by HGNC in the carbon-oxygen lyases group. UniProt lists the protein name as 6-pyruvoyl tetrahydrobiopterin synthase, and PTPS is a commonly used alias. Mutations in the gene result in hyperphenylalaninemia, which links PTS to inherited disorders of phenylalanine metabolism. Orthologues of the gene are present in mouse and rat, both named Pts, allowing the pathway to be studied in rodent models.
PTS catalyses the irreversible second step in making BH4 from GTP, so it is central to studies of this cofactor pathway.
Mutations in the PTS gene result in hyperphenylalaninemia, making the enzyme relevant to investigation of inherited disorders of phenylalanine metabolism.
BH4 is an essential cofactor for enzymes involved in serotonin biosynthesis, so PTS is relevant to work on this pathway.
BH4 regulates NO synthase activity, placing PTS upstream of this signalling system and relevant to studies of cofactor supply.
PTS catalyses the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin by eliminating inorganic triphosphate. This is the second, irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin is an essential cofactor of the aromatic amino acid hydroxylases.
PTS is the HGNC symbol for 6-pyruvoyltetrahydropterin synthase, and PTPS is a recognised alias. UniProt names the protein 6-pyruvoyl tetrahydrobiopterin synthase and places it in the PTPS family. Its enzyme classification is EC 4.2.3.12, within the carbon-oxygen lyases.
Mutations in the PTS gene result in hyperphenylalaninemia. Mouse and rat both carry an orthologous gene named Pts, so rodent systems can be used to study the pathway. Check the datasheet of any product for its validated reactivity.
Other tetrahydrobiopterin pathway enzymes, aromatic amino acid hydroxylases and NO synthases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q03393; product specifications from Assay Genie datasheets.