4a-hydroxytetrahydrobiopterin dehydratase

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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 $\rightleftharpoons$ (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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DCO, 1DCP, and 1RU0.

[edit] References

IUBMB entry for 4.2.1.96
BRENDA references for 4.2.1.96 (Recommended.)
PubMed references for 4.2.1.96
PubMed Central references for 4.2.1.96
Google Scholar references for 4.2.1.96
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: 4828–31. PMID 8444860.