+ reduced
ferredoxin
Vitamin D3 24-hydroxylase
| Vitamin D3 24-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.15.16 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| 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] It catalyses two related chemical reactions:
Calcetriol is the active form of vitamin D3 found in the kidneys.[4][5] The enzyme can further oxidise calcitetrol, leading finally to calcitroic acid.[6][7]
Calcifediol also acts as a substrate and is oxidised to the corresponding 24-hydroxy compound, secalciferol.[8]
Vitamin D3 24-hydroxylase is an oxidoreductase that uses molecular oxygen in an oxidation reaction which requires adrenal ferredoxin to transfer electrons from nicotinamide adenine dinucleotide phosphate to its cytochrome P450 active site.[9][10]
References
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Plum, Lori A.; Deluca, Hector F. (2010). "Vitamin D, disease and therapeutic opportunities". Nature Reviews Drug Discovery. 9 (12): 941–955. doi:10.1038/nrd3318. PMID 21119732.
- ↑ 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.
- ↑ Yu OB, Arnold LA (October 2016). "Calcitroic Acid-A Review". ACS Chemical Biology. 11 (10): 2665–2672. doi:10.1021/acschembio.6b00569. PMC 5074857. PMID 27574921.
- ↑ Bikle, Daniel D. (2014). "Vitamin D Metabolism, Mechanism of Action, and Clinical Applications". Chemistry & Biology. 21 (3): 319–329. doi:10.1016/j.chembiol.2013.12.016. PMC 3968073. PMID 24529992.
- ↑ Enzyme 1.14.15.16 at KEGG Pathway Database.
- ↑ 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.
External links
- Vitamin+D3+24-hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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