1.14.15.16 A326G the mutant converts 1alpha-hydroxyvitamin-D3 into 1alpha,25-dihydroxyvitamin-D3-26,23-lactone 717838 1.14.15.16 A326G the mutation converts human CYP24A1 from 25-hydroxyvitamin-D3 24-hydroxylase into 25-hydroxyvitamin-D3 23-hydroxylase, generating 1alpha,25-dihydroxyvitamin D3-26,23-lactone 716740 1.14.15.16 E143del naturally occuring mutation 736557 1.14.15.16 E147del naturally occuring mutation 736557 1.14.15.16 E149del naturally occuring mutation 736557 1.14.15.16 E151X naturally occuring mutation 736557 1.14.15.16 E322K naturally occuring mutation 736557 1.14.15.16 I500F the mutant shows quite a different metabolism of 1alpha,25-dihydroxyvitamin D3 from both human and rat CYP24A1 716274 1.14.15.16 I500L the mutant also shows the C-23 oxidation pathway 716274 1.14.15.16 I500T the mutant also shows the C-23 oxidation pathway 716274 1.14.15.16 I500V the mutant also shows the C-23 oxidation pathway 716274 1.14.15.16 L409S naturally occuring missense mutation, found on only one allele, no other mutation is found in exons or in at least 30 bp of each intron/exon junction. ThecL409S mutant has about 32% of wild-type 24-hydroxylase activity 736557 1.14.15.16 additional information development of truncated expression constructs for rat DELTA51CYP24A1. Adrenodoxin binding enhances the stability of the enzyme-substrate complex, despite lowering the ligand binding affinity of the free enzyme for calcitriol over 9fold. Truncation of CYP24A1's flexible N-terminus (DELTA51) improves the enzyme's ability to recruit substrate, without altering adrenodoxin's ability to stabilize the ligand-bound form 736701 1.14.15.16 additional information genotyping and phenotypes of diverse mutants of CYP24A1, overview 736557 1.14.15.16 additional information reconstitution of the metabolism of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] and the intermediates of the C24-oxidation pathway in a phospholipid-vesicle system. Changes to the phospholipid concentration do not affect the kinetic parameters for the metabolism of 1,25(OH)2D3 by CYP24A1, indicating that it is the concentration of substrates in the membrane phase that determines their rate of metabolism 736086 1.14.15.16 R159Q naturally occuring mutation 736557 1.14.15.16 R396W naturally occuring mutation 736557 1.14.15.16 S57D site-directed mutagenesis 736701 1.14.15.16 T416A the metabolic pattern by the mutant remains rat CYP24A1wild type 716274 1.14.15.16 T416F the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway 716274 1.14.15.16 T416I the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway 716274 1.14.15.16 T416M the mutant also shows the C-23 oxidation pathway 716274 1.14.15.16 T416S the metabolic pattern by the mutant remains rat CYP24A1wild type 716274 1.14.15.16 T416V the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway 716274 1.14.15.16 V391L the mutation converts the enzyme from a catabolic 1alpha,25-dihydroxyvitamin-D3-24-hydroxylase into an anabolic 1alpha-hydroxyvitamin-D3-25-hydroxylase. The mutant enzyme retains its basal ability to catabolize 1alpha,25-dihydroxyvitamin D3 via C24 hydroxylation 717838 1.14.15.16 V391L/A326G the 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 1alpha,25-dihydroxyvitamin-D3-26,23-lactone 717838 1.14.15.16 W210R naturally occuring mutation 736557 1.14.15.16 W268X naturally occuring mutation 736557