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
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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
- sulfonylurea
-
herbicide-inducible
- lividans
-
diterpenoids
- ferredoxins
- pombe
-
abietic
-
bioconversion
-
1alpha-hydroxyvitamin
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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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Engineering
Engineering on EC 1.14.15.22 - vitamin D 1,25-hydroxylase
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I293A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 5.4 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 3.4 mmol of product per min and mol of protein
R193A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 0.48 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 0.72 mmol of product per min and mol of protein
R193Q
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 0.33 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 0.31 mmol of product per min and mol of protein
R73A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 30.9 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 20.8 mmol of product per min and mol of protein
R73A/R84A
variant is also capable of converting vitamin D2 to its active form, that is, 1alpha,25-dihydroxyvitamin D2, via 25-hydroxyvitamin D2, with its 1alpha-hydroxylation activity toward 25-hydroxyvitamin D2 being much lower than that toward 25-hydroxyvitamin D3. The substitutions enhance both 25- and 26-hydroxylation activity toward vitamin D2. After 25-hydroxylation of vitamin D2, further hydroxylation at C26 may occur frequently without the release of 25-hydroxyvitamin D2 from the substrate-binding pocket
R73V/R84A
R84A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 75.7 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 34.5 mmol of product per min and mol of protein
R84F
mutation gives preference to the 1alpha-hydroxylation of 25-hydroxyvitamin D 3 over the 25-hydroxylation of 1alpha-hydroxyvitamin D 3, opposite to the wild type
R89A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 0.25 mmol of product per min and mol of protein, no 25-hydroxyvitamin D3 hydroxylation activity at C1alpha
S236A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 4.6 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 3.4 mmol of product per min and mol of protein
V88A
1alpha-hydroxyvitamin D3 hydroxylation activity at C25 1.52 mmol of product per min and mol of protein, 25-hydroxyvitamin D3 hydroxylation activity at C1alpha 0.34 mmol of product per min and mol of protein
highly active mutant, kinetic and crystallization data
R73V/R84A
mutant exhibits 435- and 110fold higher kcat/Km values for the 25-hydroxylation of 1alpha-hydroxyvitamin D3 and 1alpha-hydroxylation of 25-hydroxyvitamin D3, respectively, compared with the wild-type
R73V/R84A
variant is also capable of converting vitamin D2 to its active form, that is, 1alpha,25-dihydroxyvitamin D2, via 25-hydroxyvitamin D2, with its 1alpha-hydroxylation activity toward 25-hydroxyvitamin D2 being much lower than that toward 25-hydroxyvitamin D3. The substitutions enhance both 25- and 26-hydroxylation activity toward vitamin D2. After 25-hydroxylation of vitamin D2, further hydroxylation at C26 may occur frequently without the release of 25-hydroxyvitamin D2 from the substrate-binding pocket