Literature summary for 1.14.14.24 extracted from

Kaufmann, M.; Prosser, D.E.; Jones, G.
Bioengineering anabolic vitamin D-25-hydroxylase activity into the human vitamin D catabolic enzyme, cytochrome P450 CYP24A1, by a V391L mutation (2011), J. Biol. Chem., 286, 28729-28737.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling. The relative position of Val391 in the beta3a-strand of a homology model and the crystal structure of rat CYP24A1 are consistent with hydrophobic contact of Val391 and the substrate side chain near C21	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A326G	about 90% loss of activity with all substrates tested	Homo sapiens
V391L	mutation converts the enzyme from a catabolic 1alpha,25-dihydroxyvitamin D3-24-hydroxylase into an anabolic 1alpha-hydroxy-vitamin-D3-25-hydroxylase, which forms the hormone, 1alpha,25-dihydroxyvitamin D3. Mutant enzyme retains its basal ability to catabolize 1alpha,25-dihydroxyvitamin D3 via C24 hydroxylation, and can also produce calcitroic acid	Homo sapiens
V391L/A326G	mutant enzyme continues to form 1alpha,25-dihydroxyvitamin D3 from 1alpha-hydroxyvitamin D3, but this initial product is diverted via the C23 hydroxylation pathway into the 26,23-lactone. About 40-60% of wild-type activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q07973	-	-

Synonyms

Synonyms	Comment	Organism
CYP24A1	-	Homo sapiens
vitamin D-25-hydroxylase	-	Homo sapiens

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Release 2023.1 (January 2023)