6-pyruvoyltetrahydropterin synthase

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6-pyruvoyltetrahydropterin synthase

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6-pyruvoyltetrahydropterin synthase
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

In enzymology, a 6-pyruvoyltetrahydropterin synthase (PTPS) (EC 4.2.3.12) is an enzyme that catalyzes the following chemical reaction:

6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin \rightleftharpoons 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate

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.

Structural studies

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.

References

  • Milstien S, Kaufman S (1989). "The biosynthesis of tetrahydrobiopterin in rat brain. Purification and characterization of 6-pyruvoyl tetrahydropterin (2'-oxo)reductase". J. Biol. Chem. 264 (14): 8066–73. PMID 2656673. 
  • Thony B, Leimbacher W, Burgisser D, Heizmann CW (1992). "Human 6-pyruvoyltetrahydropterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme". Biochem. Biophys. Res. Commun. 189 (3): 1437–43. doi:10.1016/0006-291X(92)90235-D. PMID 1282802. 

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