1.14.14.24: vitamin D 25-hydroxylase

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For detailed information about vitamin D 25-hydroxylase, go to the full flat file.

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

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.14.24 vitamin D 25-hydroxylase

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Results	in table
5	Activating Compound
8	AA Sequence
5	Application
13	Cloned(Commentary)
14	Cofactor
2	Crystallization (Commentary)
606	Disease/ Diagnostics
5	Expression
12	General Information
4	Inhibitors
22	KM Value [mM]
16	Localization
1	Metals/Ions
5	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
26	Organism
6	Pathway
3	pH Optimum
18	Protein Variants
2	Purification (Commentary)
1	Reaction
26	Reference
26	Source Tissue
1	Specific Activity [micromol/min/mg]
51	Substrates and Products (Substrate)
6	Subunits
36	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
13	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.14.24 - vitamin D 25-hydroxylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

homology modeling. The relative position of Val391 in the beta3a-strand of a homology model and the crystal structure of rat CYP24A1 are consistent with hydrophobic contact of Val391 and the substrate side chain near C21

Homo sapiens

Q07973

717838

in complex with vitamin D3, to 1.0 A resolution. The CYP2R1 structure adopts a closed conformation with the substrate access channel being covered by the ordered B'-helix and slightly opened to the surface, which defines the substrate entrance point. The active site is lined by conserved, mostly hydrophobic residues. Vitamin D3 is bound in an elongated conformation with the aliphatic side-chain pointing toward the heme. The structure reveals the secosteroid binding mode in an extended active site

Homo sapiens

Q6VVX0

717988