6-carboxytetrahydropterin synthase
6-carboxytetrahydropterin synthase | |||||||||
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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 | ||||||||
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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
- ↑ 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. doi:10.1107/s1744309108000924. PMID 18259064.
- 1 2 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. doi:10.1021/bi9001437. PMID 19231875.
External links
- 6-carboxytetrahydropterin synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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