CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.479 | Tetrahydropterin Synthase; Chain A |
|
3.30.479.10 | 6-pyruvoyl tetrahydropterin synthase/QueD |
Domain Context
CATH Clusters
| Superfamily | 6-pyruvoyl tetrahydropterin synthase/QueD |
| Functional Family | 6-carboxy-5,6,7,8-tetrahydropterin synthase |
Enzyme Information
| 4.1.2.50 |
6-carboxytetrahydropterin synthase.
based on mapping to UniProt P65870
7,8-dihydroneopterin 3'-triphosphate + H(2)O = 6-carboxy-5,6,7,8- tetrahydropterin + acetaldehyde + triphosphate.
-!- 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.
|
UniProtKB Entries (1)
| P65870 |
QUED_ECOLI
Escherichia coli K-12
6-carboxy-5,6,7,8-tetrahydropterin synthase
|
PDB Structure
| PDB | 4NTN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Biochemical and Structural Studies of 6-Carboxy-5,6,7,8-tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity within the Tunnel-fold Superfamily.
J.Biol.Chem.
|
