1.14.15.22: vitamin D 1,25-hydroxylase
This is an abbreviated version!
For detailed information about vitamin D 1,25-hydroxylase, go to the full flat file.
Word Map on EC 1.14.15.22
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1.14.15.22
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25-hydroxylation
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1alpha-hydroxylation
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1alpha,25-dihydroxyvitamin
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25-hydroxyvitamin
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sulfonylurea
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herbicide-inducible
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lividans
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diterpenoids
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ferredoxins
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pombe
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abietic
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bioconversion
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1alpha-hydroxyvitamin
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schizosaccharomyces
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synthesis
- 1.14.15.22
-
25-hydroxylation
-
1alpha-hydroxylation
-
1alpha,25-dihydroxyvitamin
-
25-hydroxyvitamin
- sulfonylurea
-
herbicide-inducible
- lividans
-
diterpenoids
- ferredoxins
- pombe
-
abietic
-
bioconversion
-
1alpha-hydroxyvitamin
-
schizosaccharomyces
- synthesis
Reaction
+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + = + 2 oxidized ferredoxin [iron-sulfur] cluster +
Synonyms
CYP105A1, cytochrome P450SU-1, Streptomyces griseolus cytochrome P450SU-1, vitamin D3 dihydroxylase
ECTree
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Crystallization
Crystallization on EC 1.14.15.22 - vitamin D 1,25-hydroxylase
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structure of the mutant R73V/R84A with 1alpha,25-dihydroxyvitamin D3, a hydrogen-bond network including the 1alpha-hydroxyl group and several water molecules play an important role in the substrate-binding for 26-hydroxylation
wild-type to 1.5 A resolution, and mutant R84A, native protein and in complex with 1alpha,25-dihydroxyvitamin D3. The compound is positioned 11 A from the iron atom along the I helix within the pocket. The loss of two hydrogen bonds in the R84A mutant increases the adaptability of the B and F helices, creating a transient binding site