Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.15.18
Description:Calcidiol 1-monooxygenase.
Alternative Name: 25-OHD-1 alpha-hydroxylase.
25-hydroxyvitamin D-1 alpha hydroxylase.
25-hydroxyvitamin D(3) 1-alpha-hydroxylase.
25-hydroxycholecalciferol 1-monooxygenase.
25-hydroxycholecalciferol 1-hydroxylase.
Prosite: PDOC00081;
PDB:
PDBScop
Cath: 1.10.630.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.18
BRENDA Enzyme Link: BRENDA 1.14.15.18
KEGG Enzyme Link: KEGG1.14.15.18
BioCyc Enzyme Link: BioCyc 1.14.15.18
ExPASy Enzyme Link: ExPASy1.14.15.18
EC2PDB Enzyme Link: EC2PDB 1.14.15.18
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.18
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.18
IntEnz Enzyme Link: IntEnz 1.14.15.18
MEDLINE Enzyme Link: MEDLINE 1.14.15.18
MSA:

1.14.15.18;

Phylogenetic Tree:

1.14.15.18;

Uniprot:
M-CSA:
RHEA:49064 2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = calcitetrol + H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[H+;H0:10].[H+;H0:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:12].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[OH2;+0:13]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles.Tang EKY, Tieu EW, Tuckey RC2012 Oct22862690
Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli.Sawada N, Sakaki T, Kitanaka S, Takeyama K, Kato S, Inouye K1999 Nov10518789
Enzymatic properties of mouse 25-hydroxyvitamin D3 1 alpha-hydroxylase expressed in Escherichia coli.Sakaki T, Sawada N, Takeyama K, Kato S, Inouye K1999 Feb10092858

RHEA:20573 calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[H+;H0:10].[H+;H0:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:12].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[OH2;+0:13]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets.Kitanaka S, Takeyama K, Murayama A, Sato T, Okumura K, Nogami M, Hasegawa Y, Niimi H, Yanagisawa J, Tanaka T, Kato S1998 Mar 59486994
25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties.Gray RW, Omdahl JL, Ghazarian JG, DeLuca HF1972 Dec 104404596
Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles.Tang EKY, Tieu EW, Tuckey RC2012 Oct22862690
Identification of the amino acid residue of CYP27B1 responsible for binding of 25-hydroxyvitamin D3 whose mutation causes vitamin D-dependent rickets type 1.Yamamoto K, Uchida E, Urushino N, Sakaki T, Kagawa N, Sawada N, Kamakura M, Kato S, Inouye K, Yamada S2005 Aug 2615972816
Metabolism of vitamin D by human microsomal CYP2R1.Shinkyo R, Sakaki T, Kamakura M, Ohta M, Inouye K2004 Nov 515465040
Regulation of 25-hydroxyvitamin D3-1 alpha-hydroxylase and production of 1 alpha,25-dihydroxyvitamin D3 by human dendritic cells.Fritsche J, Mondal K, Ehrnsperger A, Andreesen R, Kreutz M2003 Nov 112855575
Synthesis of 1,25-dihydroxyvitamin D(3) by human endothelial cells is regulated by inflammatory cytokines: a novel autocrine determinant of vascular cell adhesion.Zehnder D, Bland R, Chana RS, Wheeler DC, Howie AJ, Williams MC, Stewart PM, Hewison M2002 Mar11856765
Metabolism of vitamin D(3) by human CYP27A1.Sawada N, Sakaki T, Ohta M, Inouye K2000 Jul 1410891358