4a-hydroxytetrahydrobiopterin dehydratase
| 4-alpha-hydroxytetrahydrobiopterin dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.96 | ||||||||
| 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 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) is an enzyme that catalyzes the chemical reaction
- (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a- hydroxypterin (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
Thus, the two substrates of this enzyme are (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a- and hydroxypterin, whereas its two products are (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxy pterin hydro-lyase [(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin-formin g]. Other names in common use include 4alpha-hydroxy-tetrahydropterin dehydratase, pterin-4alpha-carbinolamine dehydratase, and 4a-hydroxytetrahydrobiopterin hydro-lyase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DCO, 1DCP, and 1RU0.
References
- Blau N, Ghisla S, Heizmann CW (1993). "Phenylalanine hydroxylase-stimulating protein/pterin-4 alpha-carbinolamine dehydratase from rat and human liver Purification, characterization, and complete amino acid sequence". J. Biol. Chem. 268 (7): 4828–31. PMID 8444860.