Vitamin D3 24-hydroxylase
| Vitamin D3 24-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.126 | ||||||||
| 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 1.14.13.126, 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
- ↑ Masuda, S.; Strugnell, S.A.; Knutson, J.C.; St-Arnaud, R.; Jones, G. (2006). "Evidence for the activation of 1α-hydroxyvitamin D2 by 25-hydroxyvitamin D-24-hydroxylase: delineation of pathways involving 1α,24-dihydroxyvitamin D2 and 1α,25-dihydroxyvitamin D2". Biochim. Biophys. Acta. 1761 (2): 221–234. 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. (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". Mol. Pharmacol. 70 (1): 120–128. doi:10.1124/mol.106.023275. PMID 16617161.
- ↑ Sakaki, T.; Kagawa, N.; Yamamoto, K.; Inouye, K. (2005). "Metabolism of vitamin D3 by cytochromes P450". Front. Biosci. 10: 119–134. doi:10.2741/1514. PMID 15574355.
- ↑ Prosser, D.E.; Kaufmann, M.; O'Leary, B.; Byford, V.; Jones, G. (2007). "Single A326G mutation converts human CYP24A1 from 25-OH-D3-24-hydroxylase into -23-hydroxylase, generating 1α,25-(OH)2D3-26,23-lactone". Proc. Natl. Acad. Sci. USA. 104 (31): 12673–12678. 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. (2004). "Metabolism of A-ring diastereomers of 1α,25-dihydroxyvitamin D3 by CYP24A1". Biochem. Biophys. Res. Commun. 321: 774–782. 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. (2004). "Novel metabolism of 1 α,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1". Biochemistry. 43: 4530–4537. doi:10.1021/bi030207f. PMID 15078099.
- ↑ Prosser, D.E.; Jones, G. (2004). "Enzymes involved in the activation and inactivation of vitamin D". Trends Biochem. Sci. 29 (12): 664–673. doi:10.1016/j.tibs.2004.10.005. PMID 15544953.
External links
- Vitamin D3 24-hydroxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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