Biology:4a-hydroxytetrahydrobiopterin dehydratase
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Short description: Enzyme
4a-hydroxytetrahydrobiopterin dehydratase | |||||||||
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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 / QuickGO | ||||||||
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The enzyme 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) catalyzes the chemical reaction
- 4a-hydroxytetrahydrobiopterin [math]\displaystyle{ \rightleftharpoons }[/math] 6,7-dihydrobiopterin + 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 4a-hydroxytetrahydrobiopterin hydro-lyase (6,7-dihydrobiopterin-forming). Other names in common use include 4a-hydroxy-tetrahydropterin dehydratase, pterin-4α-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
- "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. 1993. PMID 8444860.
Original source: https://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin dehydratase.
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