Vitamin D3 24-hydroxylase
| Vitamin D3 24-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.15.16 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Vitamin D3 24-hydroxylase (EC 1.14.15.16, CYP24A1) is an enzyme with systematic name calcitriol,NADPH:oxygen oxidoreductase (24-hydroxylating).[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- (1) calcitriol + NADPH + H+ + O2 calcitetrol + NADP+ + H2O
- (2) calcidiol + NADPH + H+ + O2 secalciferol + NADP+ + H2O
Vitamin D3 24-hydroxylase is a heme-thiolate enzyme (P-450).
References
[edit]- ^ Masuda S, Strugnell SA, Knutson JC, St-Arnaud R, Jones G (February 2006). "Evidence for the activation of 1alpha-hydroxyvitamin D2 by 25-hydroxyvitamin D-24-hydroxylase: delineation of pathways involving 1alpha,24-dihydroxyvitamin D2 and 1alpha,25-dihydroxyvitamin D2". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1761 (2): 221–34. doi:10.1016/j.bbalip.2006.01.004. PMID 16516540.
- ^ Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T (July 2006). "Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats". Molecular Pharmacology. 70 (1): 120–8. doi:10.1124/mol.106.023275. PMID 16617161. S2CID 7458859.
- ^ Sakaki T, Kagawa N, Yamamoto K, Inouye K (January 2005). "Metabolism of vitamin D3 by cytochromes P450". Frontiers in Bioscience. 10: 119–34. doi:10.2741/1514. PMID 15574355.
- ^ Prosser DE, Kaufmann M, O'Leary B, Byford V, Jones G (July 2007). "Single A326G mutation converts human CYP24A1 from 25-OH-D3-24-hydroxylase into -23-hydroxylase, generating 1alpha,25-(OH)2D3-26,23-lactone". Proceedings of the National Academy of Sciences of the United States of America. 104 (31): 12673–8. Bibcode:2007PNAS..10412673P. doi:10.1073/pnas.0702093104. PMC 1937525. PMID 17646648.
- ^ Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K (September 2004). "Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1". Biochemical and Biophysical Research Communications. 321 (4): 774–82. doi:10.1016/j.bbrc.2004.07.040. PMID 15358094.
- ^ Sawada N, Kusudo T, Sakaki T, Hatakeyama S, Hanada M, Abe D, Kamao M, Okano T, Ohta M, Inouye K (April 2004). "Novel metabolism of 1 alpha,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1". Biochemistry. 43 (15): 4530–7. doi:10.1021/bi030207f. PMID 15078099.
- ^ Prosser DE, Jones G (December 2004). "Enzymes involved in the activation and inactivation of vitamin D". Trends in Biochemical Sciences. 29 (12): 664–73. doi:10.1016/j.tibs.2004.10.005. PMID 15544953.
External links
[edit]- Vitamin+D3+24-hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
