25-Hydroxyvitamin D3 1-alpha-hydroxylase: Difference between revisions

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VD3 1A hydroxylase is located in the [[proximal tubule]] of the [[kidney]] and a variety of other tissues, including skin ([[keratinocyte]]s), immune cells,<ref name="pmid17259988">{{cite journal | vauthors = Sigmundsdottir H, Pan J, Debes GF, Alt C, Habtezion A, Soler D, Butcher EC | title = DCs metabolize sunlight-induced vitamin D3 to 'program' T cell attraction to the epidermal chemokine CCL27 | journal = Nature Immunology | volume = 8 | issue = 3 | pages = 285–93 | date = Mar 2007 | pmid = 17259988 | doi = 10.1038/ni1433 | url = http://www.biochem.wisc.edu/courses/biochem901/secure/materials/readings/08Sigmundsdottir_etal.pdf }}</ref>  and bone ([[osteoblast]]s).<ref name="pmid20739402">{{cite journal | vauthors = Kogawa M, Findlay DM, Anderson PH, Ormsby R, Vincent C, Morris HA, Atkins GJ | title = Osteoclastic metabolism of 25(OH)-vitamin D3: a potential mechanism for optimization of bone resorption | journal = Endocrinology | volume = 151 | issue = 10 | pages = 4613–25 | date = Oct 2010 | pmid = 20739402 | doi = 10.1210/en.2010-0334 }}</ref> The [[enzyme]] catalyzes the [[hydroxylation]] of  [[Calcifediol]] to [[calcitriol]] (the bioactive form of [[Vitamin D]]):<ref name="pmid4404596">{{cite journal | vauthors = Gray RW, Omdahl JL, Ghazarian JG, DeLuca HF | title = 25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties | journal = The Journal of Biological Chemistry | volume = 247 | issue = 23 | pages = 7528–32 | date = Dec 1972 | pmid = 4404596 | doi =  }}</ref>
VD3 1A hydroxylase is located in the [[proximal tubule]] of the [[kidney]] and a variety of other tissues, including skin ([[keratinocyte]]s), immune cells,<ref name="pmid17259988">{{cite journal | vauthors = Sigmundsdottir H, Pan J, Debes GF, Alt C, Habtezion A, Soler D, Butcher EC | title = DCs metabolize sunlight-induced vitamin D3 to 'program' T cell attraction to the epidermal chemokine CCL27 | journal = Nature Immunology | volume = 8 | issue = 3 | pages = 285–93 | date = Mar 2007 | pmid = 17259988 | doi = 10.1038/ni1433 | url = http://www.biochem.wisc.edu/courses/biochem901/secure/materials/readings/08Sigmundsdottir_etal.pdf }}</ref>  and bone ([[osteoblast]]s).<ref name="pmid20739402">{{cite journal | vauthors = Kogawa M, Findlay DM, Anderson PH, Ormsby R, Vincent C, Morris HA, Atkins GJ | title = Osteoclastic metabolism of 25(OH)-vitamin D3: a potential mechanism for optimization of bone resorption | journal = Endocrinology | volume = 151 | issue = 10 | pages = 4613–25 | date = Oct 2010 | pmid = 20739402 | doi = 10.1210/en.2010-0334 }}</ref> The [[enzyme]] catalyzes the [[hydroxylation]] of  [[Calcifediol]] to [[calcitriol]] (the bioactive form of [[Vitamin D]]):<ref name="pmid4404596">{{cite journal | vauthors = Gray RW, Omdahl JL, Ghazarian JG, DeLuca HF | title = 25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties | journal = The Journal of Biological Chemistry | volume = 247 | issue = 23 | pages = 7528–32 | date = Dec 1972 | pmid = 4404596 | doi =  }}</ref>


:calcidiol + 2 reduced adrenodoxin + 2 H<sup>+</sup> + O<sub>2</sub> <math>\rightleftharpoons</math> calcitriol + 2 oxidized adrenodoxin + H<sub>2</sub>O
:calcidiol + 2 reduced [[adrenodoxin reductase|adrenodoxin]] + 2 H<sup>+</sup> + O<sub>2</sub> {{eqm}} calcitriol + 2 oxidized adrenodoxin + H<sub>2</sub>O


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* {{cite journal | vauthors = Fichna M, Zurawek M, Januszkiewicz-Lewandowska D, Fichna P, Nowak J | title = PTPN22, PDCD1 and CYP27B1 polymorphisms and susceptibility to type 1 diabetes in Polish patients | journal = International Journal of Immunogenetics | volume = 37 | issue = 5 | pages = 367–72  | date = Oct 2010 | pmid = 20518841 | doi = 10.1111/j.1744-313X.2010.00935.x }}
* {{cite journal | vauthors = Fichna M, Zurawek M, Januszkiewicz-Lewandowska D, Fichna P, Nowak J | title = PTPN22, PDCD1 and CYP27B1 polymorphisms and susceptibility to type 1 diabetes in Polish patients | journal = International Journal of Immunogenetics | volume = 37 | issue = 5 | pages = 367–72  | date = Oct 2010 | pmid = 20518841 | doi = 10.1111/j.1744-313X.2010.00935.x }}
* {{cite journal | vauthors = Wjst M, Heimbeck I, Kutschke D, Pukelsheim K | title = Epigenetic regulation of vitamin D converting enzymes | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 121 | issue = 1-2 | pages = 80–3  | date = Jul 2010 | pmid = 20304056 | doi = 10.1016/j.jsbmb.2010.03.056 }}
* {{cite journal | vauthors = Wjst M, Heimbeck I, Kutschke D, Pukelsheim K | title = Epigenetic regulation of vitamin D converting enzymes | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 121 | issue = 1-2 | pages = 80–3  | date = Jul 2010 | pmid = 20304056 | doi = 10.1016/j.jsbmb.2010.03.056 }}
* {{cite journal | vauthors = Liu CY, Wu MC, Chen F, Ter-Minassian M, Asomaning K, Zhai R, Wang Z, Su L, Heist RS, Kulke MH, Lin X, Liu G, Christiani DC | title = A Large-scale genetic association study of esophageal adenocarcinoma risk | journal = Carcinogenesis | volume = 31 | issue = 7 | pages = 1259–63  | date = Jul 2010 | pmid = 20453000 | pmc = 2893800 | doi = 10.1093/carcin/bgq092 }}
* {{cite journal | vauthors = Liu CY, Wu MC, Chen F, Ter-Minassian M, Asomaning K, Zhai R, Wang Z, Su L, Heist RS, [[Matthew Kulke|Kulke MH]], Lin X, Liu G, Christiani DC | title = A Large-scale genetic association study of esophageal adenocarcinoma risk | journal = Carcinogenesis | volume = 31 | issue = 7 | pages = 1259–63  | date = Jul 2010 | pmid = 20453000 | pmc = 2893800 | doi = 10.1093/carcin/bgq092 }}
* {{cite journal | vauthors = Sunyer J, Basagaña X, González JR, Júlvez J, Guerra S, Bustamante M, de Cid R, Antó JM, Torrent M | title = Early life environment, neurodevelopment and the interrelation with atopy | journal = Environmental Research | volume = 110 | issue = 7 | pages = 733–8  | date = Oct 2010 | pmid = 20701904 | doi = 10.1016/j.envres.2010.07.005 }}
* {{cite journal | vauthors = Sunyer J, Basagaña X, González JR, Júlvez J, Guerra S, Bustamante M, de Cid R, Antó JM, Torrent M | title = Early life environment, neurodevelopment and the interrelation with atopy | journal = Environmental Research | volume = 110 | issue = 7 | pages = 733–8  | date = Oct 2010 | pmid = 20701904 | doi = 10.1016/j.envres.2010.07.005 }}
* {{cite journal | vauthors = Simon KC, Munger KL, Ascherio A | title = Polymorphisms in vitamin D metabolism related genes and risk of multiple sclerosis | journal = Multiple Sclerosis (Houndmills, Basingstoke, England) | volume = 16 | issue = 2 | pages = 133–8  | date = Feb 2010 | pmid = 20007432 | pmc = 2819633 | doi = 10.1177/1352458509355069 }}
* {{cite journal | vauthors = Simon KC, Munger KL, Ascherio A | title = Polymorphisms in vitamin D metabolism related genes and risk of multiple sclerosis | journal = Multiple Sclerosis (Houndmills, Basingstoke, England) | volume = 16 | issue = 2 | pages = 133–8  | date = Feb 2010 | pmid = 20007432 | pmc = 2819633 | doi = 10.1177/1352458509355069 }}
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{{DEFAULTSORT:25-Hydroxyvitamin D3 1-Alpha-Hydroxylase}}
{{DEFAULTSORT:25-Hydroxyvitamin D3 1-Alpha-Hydroxylase}}
[[Category:EC 1.14.13]]
[[Category:EC 1.14.13]]
[[Category:NADPH-dependent enzymes]]
[[Category:NADPH-dependent enzymes]]
[[Category:Human proteins]]
[[Category:Human proteins]]

Latest revision as of 16:26, 26 May 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

25-Hydroxyvitamin D3 1-alpha-hydroxylase (VD3 1A hydroxylase) also known as cytochrome p450 27B1 (CYP27B1) or simply 1-alpha-hydroxylase is a cytochrome P450 enzyme that in humans is encoded by the CYP27B1 gene.[1][2][3]

VD3 1A hydroxylase is located in the proximal tubule of the kidney and a variety of other tissues, including skin (keratinocytes), immune cells,[4] and bone (osteoblasts).[5] The enzyme catalyzes the hydroxylation of Calcifediol to calcitriol (the bioactive form of Vitamin D):[6]

calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 ⇌ calcitriol + 2 oxidized adrenodoxin + H2O
calcidiol 1-monooxygenase
Identifiers
EC number1.14.15.18
CAS number9081-36-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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<imagemap> Image:VitaminDSynthesis WP1531.png
|{{{bSize}}}px|alt=Vitamin D Synthesis Pathway (view / edit)]]
Vitamin D Synthesis Pathway (view / edit)
  1. The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

References

  1. "Entrez Gene: cytochrome P450".
  2. Takeyama K, Kitanaka S, Sato T, Kobori M, Yanagisawa J, Kato S (Sep 1997). "25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis". Science. 277 (5333): 1827–30. doi:10.1126/science.277.5333.1827. PMID 9295274.
  3. Monkawa T, Yoshida T, Wakino S, Shinki T, Anazawa H, Deluca HF, Suda T, Hayashi M, Saruta T (Oct 1997). "Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase". Biochemical and Biophysical Research Communications. 239 (2): 527–33. doi:10.1006/bbrc.1997.7508. PMID 9344864.
  4. Sigmundsdottir H, Pan J, Debes GF, Alt C, Habtezion A, Soler D, Butcher EC (Mar 2007). "DCs metabolize sunlight-induced vitamin D3 to 'program' T cell attraction to the epidermal chemokine CCL27" (PDF). Nature Immunology. 8 (3): 285–93. doi:10.1038/ni1433. PMID 17259988.
  5. Kogawa M, Findlay DM, Anderson PH, Ormsby R, Vincent C, Morris HA, Atkins GJ (Oct 2010). "Osteoclastic metabolism of 25(OH)-vitamin D3: a potential mechanism for optimization of bone resorption". Endocrinology. 151 (10): 4613–25. doi:10.1210/en.2010-0334. PMID 20739402.
  6. Gray RW, Omdahl JL, Ghazarian JG, DeLuca HF (Dec 1972). "25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties". The Journal of Biological Chemistry. 247 (23): 7528–32. PMID 4404596.

Further reading

External links