6-pyruvoyltetrahydropterin synthase | |||||||
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Identifiers | |||||||
EC number | 4.2.3.12 | ||||||
CAS number | 97089-82-2 | ||||||
Databases | |||||||
IntEnz | IntEnz view | ||||||
BRENDA | BRENDA entry | ||||||
ExPASy | NiceZyme view | ||||||
KEGG | KEGG entry | ||||||
MetaCyc | metabolic pathway | ||||||
PRIAM | profile | ||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||
Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, a 6-pyruvoyltetrahydropterin synthase (PTPS) (EC 4.2.3.12) is an enzyme that catalyzes the following chemical reaction:
Hence, this enzyme has one substrate, 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin, and two products, 6-pyruvoyl-5,6,7,8-tetrahydropterin and triphosphate.
This enzyme belongs to the family of lyases, to be specific, those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Other names in common use include 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-, and dihydroxypteridine triphosphate lyase. This enzyme participates in tetrahydrobiopterin biosynthesis.
As of mid-2010, 13 structures have been solved for this class of enzymes, with PDB accession codes 3M0N, 3LZE, 3LX3, 3I2B, 2DTT, 1GTQ, 1B66, 1B6Z, 1Y13, 2A0S, 2DJ6, 2G64, and 2OBA.
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