1.14.14.24: vitamin D 25-hydroxylase
This is an abbreviated version!
For detailed information about vitamin D 25-hydroxylase, go to the full flat file.
Word Map on EC 1.14.14.24
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1.14.14.24
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25-hydroxyvitamin
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cyp27b1
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cyp2j2
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arachidonic
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25-hydroxylation
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epoxyeicosatrienoic
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epoxygenase
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rickets
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d-related
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male-specific
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7-dehydrocholesterol
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cholecalciferol
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astemizole
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ebastine
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terfenadine
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d-associated
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medicine
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1alpha-hydroxylation
- 1.14.14.24
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25-hydroxyvitamin
- cyp27b1
- cyp2j2
-
arachidonic
-
25-hydroxylation
-
epoxyeicosatrienoic
- epoxygenase
- rickets
-
d-related
-
male-specific
- 7-dehydrocholesterol
- cholecalciferol
- astemizole
- ebastine
- terfenadine
-
d-associated
- medicine
-
1alpha-hydroxylation
Reaction
Synonyms
CYP2R1, CYP24A1, CYP2C11, CYP2D25, CYP2J3, CYP2R1, CYPIIJ3, Cytochrome P450 2C11, cytochrome P450 2J2, Cytochrome P450 2J3, cytochrome P450 2R1, EC 1.14.13.159, VDH, vitamin D 25-hydroxylase, vitamin D-25-hydroxylase, vitamin D2 25-hydroxylase, vitamin D3 25-hydroxylase, vitamin D3 hydroxylase
ECTree
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Engineering
Engineering on EC 1.14.14.24 - vitamin D 25-hydroxylase
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L99P
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mutation identified in a patient with low circulating levels of 25-hydroxyvitamin D and classic symptoms of vitamin D deficiency. This individual is homozygous for a transition mutation in exon 2 of the CYP2R1 gene on chromosome 11p15.2, leading to the substitution of a proline for an evolutionarily conserved leucine and eliminating vitamin D 25-hydroxylase enzyme activity
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
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
T70R/V156L/E216M/E384R
21fold increase in hydroxylase activity
T70R/V156S/E216A/E384R
7.9fold increase in hydroxylase activity
T70R/V156L/E216M/E384R
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21fold increase in hydroxylase activity
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A241G/L243V/F244L/P245R/R246F
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mutation in substrate recognition site 3, to the equivalent residues in CYP2D6, an enzyme not active in 25-hydroxylation. The 25-hydroxylase activity of the mutant is completely lost whereas the activity toward tolterodine remains virtually unaffected
additional information
construction of null mutant enzyme-deficient Cyp2r1-/- mice, that show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
additional information
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construction of null mutant enzyme-deficient Cyp2r1-/- mice, that show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
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