6-carboxytetrahydropterin synthase

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6-carboxytetrahydropterin synthase
4ntn.jpg
6-Carboxy-5,6,7,8-tetrahydropterin synthase hexamer, E.Coli
Identifiers
EC number 4.1.2.50
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

6-carboxytetrahydropterin synthase (EC 4.1.2.50, CPH4 synthase, queD (gene), ToyB , ykvK (gene)) is an enzyme with systematic name 7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming).[1][2] This enzyme catalyses the following ((chemical reaction))

7,8-dihydroneopterin 3'-triphosphate + H2O 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate

This enzyme binds Zn2+. It is isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine. The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin.[2]

References[edit]

  1. ^ Cicmil, N.; Shi, L. (2008). "Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64: 119–122. PMC 2374184Freely accessible. PMID 18259064. doi:10.1107/s1744309108000924. 
  2. ^ a b McCarty, R.M; Somogyi, A.; Bandarian, V. (2009). "Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase". Biochemistry. 48: 2301–2303. PMC 3227869Freely accessible. PMID 19231875. doi:10.1021/bi9001437. 

External links[edit]