| 6-carboxytetrahydropterin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 6-Carboxy-5,6,7,8-tetrahydropterin synthase hexamer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 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 reversible 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 stimulation 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]
- ^ Cicmil N, Shi L (February 2008). "Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis". Acta Crystallographica Section F. 64 (2): 119–22. doi:10.1107/s1744309108000924. PMC 2374184. PMID 18259064.
- ^ a b McCarty RM, Somogyi A, Bandarian V (March 2009). "Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase". Biochemistry. 48 (11): 2301–3. doi:10.1021/bi9001437. PMC 3227869. PMID 19231875.
External links[edit]
Media related to 6-carboxytetrahydropterin synthase at Wikimedia Commons- 6-carboxytetrahydropterin+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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