Literature summary for 1.14.15.16 extracted from

Ferla, S.; Aboraia, A.S.; Brancale, A.; Pepper, C.J.; Zhu, J.; Ochalek, J.T.; DeLuca, H.F.; Simons, C.
Small-molecule inhibitors of 25-hydroxyvitamin D-24-hydroxylase (CYP24A1): synthesis and biological evaluation (2014), J. Med. Chem., 57, 7702-7715.

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	synthesis of imidazole styrylbenzamide, tert-butyl styrylimidazole, and tert-butyl styrylsulfonate derivatives and evaluation of binding affinity and inhibitory activity against CYP24A1. Imidazole styrylbenzamides are potent inhibitors of CYP24A1, having selectivity with respect to CYP27B1 comparable with or greater than that of the standard ketoconazole. The compounds reach the active site through the vitamin D access tunnel and are exposed to multiple hydrophobic residues. The imidazole styrylbenzamides are optimally positioned to allow interaction of the imidazole with the heme, and, in the case of the methoxy derivatives, a hydrogen bond between the 3-methoxy group and Gln82 stabilizes the molecule in a favorable active conformation. Docking study, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q07973	gene CYP24A1	-

Synonyms

Synonyms	Comment	Organism
25-hydroxyvitamin D-24-hydroxylase	-	Homo sapiens
CYP24A1	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	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	Homo sapiens

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Release 2023.1 (January 2023)