Cytochrome P450 2R1

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Cytochrome P450 2R1
Cytochrome P450 2R1
Crystal structure of cytochrome P450 2R1 according to PDB  2ojd

Existing structural data : PDB  2ojd , 3c6g

Properties of human protein
Mass / length primary structure 501 amino acids
Cofactor Heme thiolate
Identifier
Gene name CYP2R1
External IDs
Enzyme classification
EC, category 1.14.13.15 ,  oxygenase
Response type Hydroxylation
Substrate 3α, 7α, 12α-trihydroxy-5β-cholestane
Products 3α, 7α, 12α, 26-tetrahydroxy-5β-cholestane
Occurrence
Parent taxon Vertebrates

Cytochrome P450 2R1 (CYP2R1) (also: vitamin D - 25-hydroxylase ) is the enzyme that hydroxylates vitamin D to calcidiol . This response is the first of two in the biosynthesis of the hormone calcitriol ; in all vertebrates, including humans, it takes place exclusively in the microsomes of the liver . Mutations in CYP2R1 - gene can enzyme deficiency, and this to a rare inherited form of rickets lead.

In a study of 200 diabetes 1 patients, CYP2R1 variants were associated with low vitamin D levels.

Catalyzed reaction

D3+ NADPH / H + + O 2 ⇒
⇒ Calcidiol+ NADP + + H 2 O

Vitamin D3 is hydroxylated to calcidiol. Vitamin D2 is also accepted as a substrate .

Individual evidence

  1. ↑ Nelson DR: Comparison of P450s from human and fugu: 420 million years of vertebrate P450 evolution . In: Arch. Biochem. Biophys. . 409, No. 1, January 2003, pp. 18-24. PMID 12464240 .
  2. ↑ UniProt Q6VVX0
  3. ↑ Ramos-Lopez E, Brück P, Jansen T, Herwig J, Badenhoop K: CYP2R1 (vitamin D 25-hydroxylase) gene is associated with susceptibility to type 1 diabetes and vitamin D levels in Germans . In: Diabetes Metab. Res. Rev. . 23, No. 8, November 2007, pp. 631-6. doi : 10.1002 / dmrr.719 . PMID 17607662 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Vitamin D Metabolism  - Learning and Teaching Materials