1.14.15.16: vitamin D3 24-hydroxylase
This is an abbreviated version!
For detailed information about vitamin D3 24-hydroxylase, go to the full flat file.
Word Map on EC 1.14.15.16
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1.14.15.16
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cyp24a1
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parathyroid
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1alpha-hydroxylase
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rickets
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24,25-dihydroxyvitamin
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hypercalcemia
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24-hydroxylation
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retinoids
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d-dependent
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1alpha,25oh2d3
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osteocalcin
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vdres
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d-deficient
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1-hydroxylase
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d-responsive
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1,25-dihydroxycholecalciferol
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hyperparathyroidism
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ketoconazole
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nephrocalcinosis
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alopecia
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vdr-mediated
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hypophosphatemic
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d-binding
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1,25oh2d3-induced
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extrarenal
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hypercalciuria
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cholecalciferol
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25-hydroxycholecalciferol
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calcemic
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1alpha-ohase
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alpha-hydroxyvitamin
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calcidiol
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d-resistant
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d3-1alpha-hydroxylase
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osteomalacia
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d-replete
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secosteroid
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hvdrr
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sodium-phosphate
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medicine
- 1.14.15.16
- cyp24a1
- parathyroid
-
1alpha-hydroxylase
- rickets
-
24,25-dihydroxyvitamin
- hypercalcemia
-
24-hydroxylation
-
retinoids
-
d-dependent
-
1alpha,25oh2d3
- osteocalcin
-
vdres
-
d-deficient
- 1-hydroxylase
-
d-responsive
- 1,25-dihydroxycholecalciferol
- hyperparathyroidism
- ketoconazole
- nephrocalcinosis
- alopecia
-
vdr-mediated
-
hypophosphatemic
-
d-binding
-
1,25oh2d3-induced
-
extrarenal
-
hypercalciuria
- cholecalciferol
- 25-hydroxycholecalciferol
-
calcemic
- 1alpha-ohase
-
alpha-hydroxyvitamin
- calcidiol
-
d-resistant
-
d3-1alpha-hydroxylase
-
osteomalacia
-
d-replete
-
secosteroid
-
hvdrr
-
sodium-phosphate
- medicine
Reaction
+ 2 reduced adrenodoxin + 2 H+ + = + 2 oxidized adrenodoxin +
Synonyms
1,25-(OH)2D3-24-hydroxylase, 1,25-dihydroxyvitamin D3 24-hydroxylase, 1alpha,25-dihydroxyvitamin D3 24-hydroxylase, 24-hydroxylase, 24-OHase, 24OHase, 25-hydroxyvitamin D-24-hydroxylase, 25-hydroxyvitamin D3-24-hydroxylase, 25-OH-D3-24-hydroxylase, CYP24A1, cytochrome P450 24A1, EC 1.14.13.126, P450cc24, vitamin D 24-hydroxylase, vitamin D-24-hydroxylase
ECTree
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Engineering
Engineering on EC 1.14.15.16 - vitamin D3 24-hydroxylase
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A326G
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
V391L
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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
V391L/A326G
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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
I500F
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the mutant shows quite a different metabolism of 1alpha,25-dihydroxyvitamin D3 from both human and rat CYP24A1
T416F
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the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway
T416I
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the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway
T416V
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the mutant has reaction specificity similar to human CYP24A1 by also showing the C-23 oxidation pathway
additional information
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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
A326G
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the mutant converts 1alpha-hydroxyvitamin-D3 into 1alpha,25-dihydroxyvitamin-D3-26,23-lactone
genotyping and phenotypes of diverse mutants of CYP24A1, overview
additional information
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genotyping and phenotypes of diverse mutants of CYP24A1, overview
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
additional information
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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