EC Number   |
General Information |
Reference |
|---|
   1.14.15.16 | malfunction |
mutations of the CYP24A1 gene encoding the 24-hydroxylase that inactivates metabolites of vitamin D can cause hypercalcemia in infants and adults, phenotypes, overview. A young adult with a CYP24A1 mutation L409S shows bilateral nephrolithiasis and hypercalcemia in the setting of excessive vitamin D intake |
736557 |
| 1.14.15.16 | malfunction |
natural inactivating mutations of CYP24A1 cause the genetic disease idiopathic infantile hypercalcemia |
726809 |
| 1.14.15.16 | malfunction |
the Cyp24a1 knockout mouse is consistent with a catabolic role for CYP24A1, because it shows poor viability, 50% of homozygous mice die before weaning, showing hypercalcemia and signs of renal calcification. Isolated cultured keratinocytes from Cyp24a1-deficient mice fail to synthesize calcitroic acid |
716973 |
| 1.14.15.16 | metabolism |
CYP24A1 proceeds mainly through the C-24 oxidation pathway, resulting in its conversion into a side-chain cleaved inactive water-soluble metabolite, calcitroic acid. Isolation and identification of 3-epi-calcitroic acid as the final inactive metabolite of 3-epi-1alpha,25(OH)2D3 produced by rat CYP24A1. The amount of 3-epi-calcitroic acid produced from 3-epi-1alpha,25(OH)2D3 is threefold less than that of calcitroic acid, the analogous final inactive metabolite produced from 1alpha,25(OH)2D3, due to a slower oxidation reaction with the epimer. Molecular docking analysis using the crystal structure of rat CYP24A1 reveals that 3-epi-1alpha,25(OH)2D3, unlike 1alpha,25(OH)2D3, binds to CYP24A1 in an alternate configuration that destabilizes the formation of the enzyme-substrate complex sufficiently to slow the rate at which 3-epi-1alpha,25(OH)2D3 is inactivated by CYP24A1 through its metabolism into 3-epi-calcitroic acid. Metabolism of 1alpha,25(OH)2D3 into 3-epi-1alpha,25(OH)2D3 through the C-3 epimerization pathway, overview |
736545 |
| 1.14.15.16 | metabolism |
P450cc24 is a multicatalytic enzyme catalyzing most, if not all, of the reactions in the C-24/C-23 pathway of 25-hydroxyvitamin D3 (calcidiol) metabolism |
714138 |
| 1.14.15.16 | more |
evaluation of the 3,5-dimethoxy and 3,4,5-trimethoxy derivatives of imidazole styrylbenzamide in chronic lymphocytic leukemia cells reveals that co-treatment of 1alpha,25-dihydroxyvitamin D3 plus inhibitor coordinately upregulates GADD45alpha and CDKN1A |
736616 |
| 1.14.15.16 | physiological function |
CYP24A1 can activate and inactivate vitamin D prodrugs in skin and other target cells in vitro |
714302 |
| 1.14.15.16 | physiological function |
CYP24A1 has a crucial role in vitamin D inactivation in vivo |
716973 |
| 1.14.15.16 | physiological function |
CYP24A1 is a multicatalytic enzyme that sequentially oxidizes the side chain of 1alpha,25-dihydroxyvitamin D3, leading to loss of its hormonal activity. 3-Epi-1alpha,25-dihydroxyvitamin D3 (3-epi-1alpha,25(OH)2D3), a natural metabolite of 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3), exhibits potent vitamin D receptor-mediated actions such as inhibition of keratinocyte growth or suppression of parathyroid hormone secretion |
736545 |
| 1.14.15.16 | physiological function |
CYP24A1 is the multicatalytic cytochrome P450 responsible for the catabolism of vitamin D via the C23- and C24-oxidation pathways. CYP24A1 is a membrane-bound hemoprotein which utilizes the electrons from NADPH via a transport chain comprising adrenodoxin and adrenodoxin reductase. Inactivation of 1,25(OH)2D3 by CYP24A1 via the C24-oxidation pathway |
736086 |
