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Information on EC 1.14.15.18 - calcidiol 1-monooxygenase
for references in articles please use BRENDA:EC1.14.15.18
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EC Tree 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
1.14.15.18 calcidiol 1-monooxygenase
IUBMB Comments
A P-450 (heme-thiolate) enzyme found in mammals.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.14.15.18
-
1,25-dihydroxyvitamin
- cyp24a1
- parathyroid
- calcitriol
- rickets
-
24-hydroxylase
- phosphorus
- hypercalcemia
- osteoblast
-
d-dependent
-
extrarenal
-
autocrine
- hyperparathyroidism
-
1alpha,25oh2d3
-
hypophosphatemic
- osteomalacia
- klotho
-
d-deficient
- 24-ohase
-
d-related
- hydroxylases
-
vdr-mediated
-
phosphaturic
- 1,25-dihydroxycholecalciferol
- hyperphosphatemia
-
secosteroids
-
factor-23
-
25-hydroxylation
- cathelicidin
-
hypocalcemic
-
calcemic
-
intracrine
-
prodifferentiating
-
d3-24-hydroxylase
-
sodium-phosphate
- 7-dehydrocholesterol
- medicine
-
d-binding
-
casrs
-
hypercalciuria
-
hypovitaminosis
-
calbindin-d9k
-
vdres
-
non-renal
-
megalin
Reaction Schemes
show+
2
reduced adrenodoxin
+
2
+
=
+
2
+
Synonyms
cyp27b1, 1alpha-hydroxylase, 1alpha-ohase, 1-ohase, 25-hydroxyvitamin d-1alpha-hydroxylase, 25-hydroxyvitamin d-1 alpha-hydroxylase, cyp1alpha, 25-hydroxyvitamin d 1alpha-hydroxylase, 25-hydroxyvitamin d3-1alpha-hydroxylase, 25-hydroxyvitamin d3 1alpha-hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-hydroxylase-25-hydroxyvitamin D3
-
-
-
-
1alpha-hydroxylase
1alphaOHase
25-hydroxy D3-1alpha-hydroxylase
-
-
-
-
25-hydroxycholecalciferol 1-hydroxylase
-
-
-
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25-hydroxycholecalciferol 1-monooxygenase
-
-
-
-
25-hydroxycholecalciferol 1alpha-hydroxylase
-
-
-
-
25-hydroxycholecalciferol-1-hydroxylase
-
-
-
-
25-hydroxyvitamin D-1alpha-hydroxylase
25-hydroxyvitamin D3 1alpha-hydroxylase
25-hydroxyvitamin D3-1alpha-hydroxylase
CYB27B1
CYP27B1
EC 1.14.13.13
-
-
formerly
-
hydroxylase, 25-hydroxcholecalciferol 1-
-
-
-
-
oxygenase, 25-hydroxycholecalciferol 1-mono-
-
-
-
-
vitamin D3 25- and 1alpha-hydroxylase
-
i.e. CYP2D25, microsomal, higher 25-hydroxylating than 1alpha-hydroxylating activity
25-hydroxyvitamin D-1alpha-hydroxylase
-
-
25-hydroxyvitamin D3 1alpha-hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstitution of the enzyme system in E. coli cells, consisting of NADH-adrenodoxin reductase, adrenodoxin and CYP27B1
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstitution of the enzyme system in E. coli cells, consisting of NADH-adrenodoxin reductase, adrenodoxin and CYP27B1
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
25-hydroxyvitamin D3 1alpha-hydroxylase is a cytochrome P-450-dependent mixed-function oxidase
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
25-hydroxyvitamin D3 1alpha-hydroxylase is a cytochrome P-450-dependent mixed-function oxidase
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
25-hydroxyvitamin D3 1alpha-hydroxylase is a cytochrome P-450-dependent mixed-function oxidase
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
25-hydroxyvitamin D3 1alpha-hydroxylase is a cytochrome P-450-dependent mixed-function oxidase
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
amino acid composition and terminal sequence determination
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
cytochrome P-450 enzyme
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
cytochrome P-450 enzyme
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
cytochrome P-450 enzyme
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
amino acid sequence determination
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
kidney mitochondrial 25-hydroxyvitamin D3-1alpha-hydroxylation system consists of a renal ferredoxin reductase (flavoprotein), renal ferredoxin and cytochrome P-450
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
reconstituted with cytochrome P-450, adrenal ferredoxin, i.e. adrenodoxin, and adrenodoxin reductase
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
cytochrome P-450 type is specific for hydroxylation site of 25-hydroxyvitamin D3
-
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
enzyme can be reconstituted with the 3 components: cytochrome P-450D1alpha, NADPH-renodoxin reductase and renodoxin
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
ferredoxin, ferredoxin reductase and cytochrome P-450
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
ferredoxin, ferredoxin reductase and cytochrome P-450
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
ferredoxin, ferredoxin reductase and cytochrome P-450
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calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
vitamin D3 biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
calcidiol,adrenodoxin:oxygen oxidoreductase (1-hydroxylating)
A P-450 (heme-thiolate) enzyme found in mammals.
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CAS REGISTRY NUMBER
COMMENTARY
9081-36-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
(24R),25-dihydroxyvitamin D3 + NADPH + O2
1alpha,24,25-trihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
1alpha-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
20-hydroxyvitamin D3 + NADPH + O2
1alpha,20-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
24,25-dihydroxycholecalciferol + reduced adrenodoxin + O2
1alpha,24,25-trihydroxycholecalciferol + oxidized adrenodoxin + H2O
-
Substrates: -
Products: -
Products: -
r
25-hydroxyvitamin D2 + NADPH + H+ + O2
1,25-dihydroxyvitamin D2 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + H+ + O2
25-hydroxyvitamin D3 + H2O
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + H+ + O2
1,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
cholecalciferol + NADPH + O2
25-hydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: higher activity than with 25-hydroxycholecalciferol
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: reconstituted system
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: higher activity than with 25-hydroxycholecalciferol
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: recombinant enzyme
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: higher activity than with 25-hydroxycholecalciferol
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
23,25-dihydroxycholecalciferol + NADPH + O2
?
-
Substrates: low activity
Products: -
Products: -
?
23,25-dihydroxycholecalciferol + NADPH + O2
?
-
Substrates: recombinant enzyme
Products: -
Products: -
?
24-oxo-23,25-dihydroxycholecalciferol + NADPH + O2
?
-
Substrates: low activity
Products: -
Products: -
?
24-oxo-23,25-dihydroxycholecalciferol + NADPH + O2
?
-
Substrates: recombinant enzyme
Products: -
Products: -
?
24-oxo-25-hydroxycholecalciferol + NADPH + O2
?
-
Substrates: low activity, reconstituted system
Products: -
Products: -
?
24-oxo-25-hydroxycholecalciferol + NADPH + O2
?
-
Substrates: recombinant enzyme
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: energy-dependent transhydrogenation is of importance
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: enzyme activity is correlated with phosphate content in serum
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
Substrates: the enzyme hydroxylates the major circulating form of vitamin D to the active systemic hormone 1,25(OH)2D3, local production of 1,25(OH)2D3 appears to occur also at other sites where 1alpha-hydroxylase is expressed for autocrine/paracrine regulation, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
Substrates: substrate activation by the rate-limiting enzyme 1alpha-hydroxylase in cells of the immune system under control of immune stimuli, such as interferon-gamma, in pathological situations, such as sarcoidosis, this can lead to systemic excess of 1,25(OH)2D3 and hypercalcemia
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: 1,25-dihydroxyvitamin D3 (1,25-D3) is a key determinant of calcium homeostasis, cell proliferation and differentiation, calcium and vitamin D might have a protective function against colorectal tumor pathogenesis, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: bioactivation
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: the enzyme is involved in the vitamin D signaling pathway in colonic epithelial cell differentiation by butyrate, mechanism, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: the enzyme is responsible for final hydroxylation of vitamin D3, in response to IFNgamma and CD14/TLR4 activation
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: extra-renal functions of 1alpha-hydroxylase in vitamin D physiology, regulation, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: 1,25(OH)2D3 is an antiproliferative agent that may inhibit proliferation of breast cancer cells
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: regulation of enzyme expression in kidney proximal tubules, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: deficiency of the enzyme, due to mutation of residues Q65 and T409, in substrate binding causes vitamin D-dependent rickets type 1, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: binding of 25-hydroxyvitamin D3 in a structural pocket involving residues Q65, S408, and T409, molecular modeling and substrate docking
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D, involved in tumor suppressing activity due to the tumor growth inhibiting effect of 1alpha,25-dihydroxyvitamin D3
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
285537, 440101, 440102, 440103, 440104, 440105, 440108, 440109, 440110, 440111, 440113, 440121, 440123
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant enzyme
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: enzyme shows vitamin D3 25- and 1alpha-hydroxylase activity
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
calcidiol + NADPH + O2
calcitriol + NADP+ + H2O
Substrates: highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
Products: calcitriol is identical with 1,25-dihydroxycholecalciferol
?
additional information
?
-
-
Substrates: not: cholecalciferol, dihydrotachysterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 25-hydroxy group is essential for 1alpha-hydroxylating activity, the 24-hydroxy group enhances the activity, the 23-hydroxy group strongly reduces activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: not active with (23S),25-dihydroxycholecalciferol and 24-oxo-23,25-dihydroxycholecalciferol
Products: -
Products: -
?
additional information
?
-
-
Substrates: colonic and renal vitamin D hydroxylases are regulated independently
Products: -
Products: -
?
additional information
?
-
-
Substrates: 25(OH)D3 therapy is useful for colorectal cancer chemoprevention but provitamin D is less likely to be useful for colorectal cancer chemotherapy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in local production of 1alpha,25-dihydroxyvitamin D, i.e. 1alpha,25(OH)2D3, in tumorigenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: both butyrate and 1alpha-25(OH)2D3 stimulate differentiation of Caco-2 cells, while 25(OH)2D3 has no impact on cell differentiation
Products: -
Products: -
?
additional information
?
-
-
Substrates: immune regulation of the enzyme in monocytes, cross-talk between the JAK-STAT, the NFkappaB, and the p38 MAPK pathways is necessary, and direct binding of C/EBPbeta to its recognition sites in the promoter of the 1alpha-hydroxylase gene is a prerequisite, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: functional analysis of vitamin D metabolism in cancer, locally synthesized 1,25(OH)2D3 may be inefficient in preventing tumor progression, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 1alpha-OHase gene is a tumor suppressor gene responsible for the normal regulation of prostate cell growth
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 25-hydroxy group is essential for 1alpha-hydroxylating activity, the 24-hydroxy group enhances the activity, the 23-hydroxy group strongly reduces activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 25-hydroxy group is essential for 1alpha-hydroxylating activity, the 24-hydroxy group enhances the activity, the 23-hydroxy group strongly reduces activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 24,25,26,27-tetranor-23-hydroxyvitamin D3 and vitamin D3
Products: -
Products: -
?
additional information
?
-
-
Substrates: PTH and PTHrP are involved in enzyme regulation, PTH is the major protein hormone regulating calcium homeostasis, PTHrP is a PTH-like factor responsible for humoral hypercalcemia of malignancy, both peptides are required to achieve normal fetal skeletal morphogenesis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 1alpha,25(OH)2-19-nor-D3 is not converted to 1alpha,25(OH)2-19-nor-D3 by CYP27B1
Products: -
Products: -
?
additional information
?
-
-
Substrates: 25-hydroxyvitamin D3 and 25-hydroxyvitamin D2 in vesicles undergo 1alpha-hydroxylation with similar kinetics. CYP27B1 also catalyzes 1alpha-hydroxylation of vesicle-associated 24R,25-dihydroxyvitamin D3 and 20-hydroxyvitamin D3, and 25-hydroxylation of 1alpha-hydroxyvitamin D3 and 1alpha-hydroxyvitamin D2, but with much lower efficiency than for 25(OH)D3, reactions in reconstituted phospholipid vesicles with the substrates associating to the membrane, effect of vesicle phospholipid composition on metabolism of 25(OH)D3 by CYP27B1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: a multifunctional enzyme catalyzing also the reaction of cholestanetriol 26-monooxygenase, EC 1.14.13.15, as well as oxidation of 5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol into the corresponding C27-acid, and the 24- and 25-hydroxylation of cholesterol, the truncated enzyme form is less efficient than the full-length CYP27A in the 27-hydroxylation of C27-sterols, and much less efficient in the 25-hydroxylation of 1alpha-hydroxyvitamin D3
Products: -
Products: -
?
additional information
?
-
-
Substrates: Vdh, a cytochrome P450 enzyme, is responsible for the biocatalytic conversion of vitamin D3, catalyzing the two-step hydroxylation of VD3, i.e. the conversion of VD3 to 25-hydroxyvitamin D3 (25(OH)VD3) and then of 25(OH)VD3 to 1alpha,25(OH)2VD3, a hormonal form of VD3. Anti-parallel substrate binding modes enable sequential hydroxylation, structure-function analysis, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
25-hydroxyvitamin D2 + NADPH + H+ + O2
1,25-dihydroxyvitamin D2 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + H+ + O2
25-hydroxyvitamin D3 + H2O
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + H+ + O2
1,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
cholecalciferol + NADPH + O2
25-hydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
(24R),25-dihydroxycholecalciferol + NADPH + O2
1alpha,24,25-trihydroxycholecalciferol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: energy-dependent transhydrogenation is of importance
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: enzyme activity is correlated with phosphate content in serum
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: recombinant in E. coli
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: central role in calcium regulation
Products: -
Products: -
?
25-hydroxycholecalciferol + NADPH + O2
calcitriol + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
Substrates: the enzyme hydroxylates the major circulating form of vitamin D to the active systemic hormone 1,25(OH)2D3, local production of 1,25(OH)2D3 appears to occur also at other sites where 1alpha-hydroxylase is expressed for autocrine/paracrine regulation, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
Substrates: substrate activation by the rate-limiting enzyme 1alpha-hydroxylase in cells of the immune system under control of immune stimuli, such as interferon-gamma, in pathological situations, such as sarcoidosis, this can lead to systemic excess of 1,25(OH)2D3 and hypercalcemia
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: 1,25-dihydroxyvitamin D3 (1,25-D3) is a key determinant of calcium homeostasis, cell proliferation and differentiation, calcium and vitamin D might have a protective function against colorectal tumor pathogenesis, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: bioactivation
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: the enzyme is involved in the vitamin D signaling pathway in colonic epithelial cell differentiation by butyrate, mechanism, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: the enzyme is responsible for final hydroxylation of vitamin D3, in response to IFNgamma and CD14/TLR4 activation
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: extra-renal functions of 1alpha-hydroxylase in vitamin D physiology, regulation, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: 1,25(OH)2D3 is an antiproliferative agent that may inhibit proliferation of breast cancer cells
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: regulation of enzyme expression in kidney proximal tubules, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: deficiency of the enzyme, due to mutation of residues Q65 and T409, in substrate binding causes vitamin D-dependent rickets type 1, overview
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D + NADPH + O2
1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D, involved in tumor suppressing activity due to the tumor growth inhibiting effect of 1alpha,25-dihydroxyvitamin D3
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Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: final step of the activation of vitamin D
Products: -
Products: -
?
25-hydroxyvitamin D3 + NADPH + O2
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: colonic and renal vitamin D hydroxylases are regulated independently
Products: -
Products: -
?
additional information
?
-
-
Substrates: 25(OH)D3 therapy is useful for colorectal cancer chemoprevention but provitamin D is less likely to be useful for colorectal cancer chemotherapy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in local production of 1alpha,25-dihydroxyvitamin D, i.e. 1alpha,25(OH)2D3, in tumorigenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: both butyrate and 1alpha-25(OH)2D3 stimulate differentiation of Caco-2 cells, while 25(OH)2D3 has no impact on cell differentiation
Products: -
Products: -
?
additional information
?
-
-
Substrates: immune regulation of the enzyme in monocytes, cross-talk between the JAK-STAT, the NFkappaB, and the p38 MAPK pathways is necessary, and direct binding of C/EBPbeta to its recognition sites in the promoter of the 1alpha-hydroxylase gene is a prerequisite, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: functional analysis of vitamin D metabolism in cancer, locally synthesized 1,25(OH)2D3 may be inefficient in preventing tumor progression, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 1alpha-OHase gene is a tumor suppressor gene responsible for the normal regulation of prostate cell growth
Products: -
Products: -
?
additional information
?
-
-
Substrates: PTH and PTHrP are involved in enzyme regulation, PTH is the major protein hormone regulating calcium homeostasis, PTHrP is a PTH-like factor responsible for humoral hypercalcemia of malignancy, both peptides are required to achieve normal fetal skeletal morphogenesis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: Vdh, a cytochrome P450 enzyme, is responsible for the biocatalytic conversion of vitamin D3, catalyzing the two-step hydroxylation of VD3, i.e. the conversion of VD3 to 25-hydroxyvitamin D3 (25(OH)VD3) and then of 25(OH)VD3 to 1alpha,25(OH)2VD3, a hormonal form of VD3. Anti-parallel substrate binding modes enable sequential hydroxylation, structure-function analysis, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
25-hydroxy-3-deoxy-2-oxavitamin D3
-
vitamin D3 analogue, competitive inhibition
25-hydroxyvitamin D2
-
CYP27B1 shows inhibition when substrate concentrations in the membrane are greater than 4 times Km, more pronounced with 25-hydroxyvitamin D3 than with 25-hydroxyvitamin D2
25-hydroxyvitamin D3
-
CYP27B1 shows inhibition when substrate concentrations in the membrane are greater than 4 times Km, more pronounced with 25-hydroxyvitamin D3 than with 25-hydroxyvitamin D2
3-deoxy-2-oxa-9(11)-didehydro-25-hydroxyvitamin D3
-
vitamin D3 analogue, competitive inhibition
A-homo-3-deoxy-2-oxa-25-hydroxyvitamin D3
-
vitamin D3 analogue, competitive inhibition
Epidermal growth factor
-
decreases mRNA expression in less differentiated cells like Caco-2/AQ and COGA-1A and -1E; i.e. EGF
1,25-Dihydroxycholecalciferol
-
calcitriol; decreases mRNA expression in less differentiated cells like Caco-2/AQ and COGA-1A and -1E
1,25-Dihydroxycholecalciferol
calcitriol; in vivo only inhibitory in vitamin D receptor containing cells, therefore: negative feedback inhibition is mediated by the enzyme through liganded vitamin D receptor
antimycin A
-
higher inhibition rate with succinate as electron donor than with malate
antimycin A
-
inhibition occurs with succinate reaction support, no inhibition together with malate
dinitrophenol
-
higher inhibition rate with malate as electron donor than with succinate
additional information
-
inhibition by renal mitochondrial protein kinase-catalyzed phosphorylation
-
additional information
-
overview, inhibitory potency of several vitamin D3 analogues
-
additional information
inhibitory effects of the MEK inhibitor PD98059, p38 MAPK inhibitor SB203580, and JNK inhibitor SP600125 on the IFNgamma/PMA-induced or IFNgamma/LPS-induced 1alpha-hydroxylase mRNA expression in THP1 cells, overview
-
additional information
-
inhibitory effects of the MEK inhibitor PD98059, p38 MAPK inhibitor SB203580, and JNK inhibitor SP600125 on the IFNgamma/PMA-induced or IFNgamma/LPS-induced 1alpha-hydroxylase mRNA expression in THP1 cells, overview
-
additional information
-
the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,25-Dihydroxycholecalciferol
-
increases mRNA expression in highly differentiated cells like Caco-2/15
adrenodoxin
-
mouse and bovine adrenodoxin display similar abilities to support CYP27B1 activity
Epidermal growth factor
-
increases mRNA expression in highly differentiated cells like Caco-2/15
additional information
-
treatment of cells with parathyroid hormone, estradiol-17beta, raloxifene, genistein, biochainin A, or 6-carboxy biochainin A increases cellular mRNA-level
-
additional information
-
5-aza-2-deoxycytidine together with trichostatin A increases mRNA expression in DU-145 cells
-
additional information
EB1285, a non-1alpha-hydroxylated vitamin D analogue prodrug of EB1089, shows about 20% ketoconazole-sensitive transcription activation of the enzyme
-
additional information
phorbol myristate acetate, lipopolysaccharide, and IFNgamma induce enzyme expression in monocytes, regulation, the induction essentially requires the JAK-STAT, NF-kappaB, and p38 MAPK pathways, chromatin remodeling is required for immune-mediated up-regulation of 1alpha-hydroxylase, overview
-
additional information
-
phorbol myristate acetate, lipopolysaccharide, and IFNgamma induce enzyme expression in monocytes, regulation, the induction essentially requires the JAK-STAT, NF-kappaB, and p38 MAPK pathways, chromatin remodeling is required for immune-mediated up-regulation of 1alpha-hydroxylase, overview
-
additional information
-
butyrate transiently upregulates enzyme expression 2.3fold
-
additional information
-
enzyme expression in monocytes is synergistically induced by IFNgamma and CD14/TLR4 ligation and paralleled by 1,25(OH)2D3 production, the induction essentially requires the JAK-STAT, NF-kappaB, and p38 MAPK pathways, expression analysis, overview
-
additional information
-
dietary calcium and vitamin D depletion induces the enzyme expression
-
additional information
-
the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26
(24R),25-dihydroxyvitamin D3
-
pH 7.4, 37°C, Michaelis-Menten kinetic parameters
49
20-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
4.8
25-hydroxyvitamin D2
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
9.7
25-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
additional information
additional information
-
Michaelis-Menten kinetics, and by a kinetic model with substrate binding at two inhibitory sites, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
(24R),25-dihydroxyvitamin D3
-
pH 7.4, 37°C, Michaelis-Menten kinetic parameters
0.14
20-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
0.82
25-hydroxyvitamin D2
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
0.92
25-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
(24R),25-dihydroxyvitamin D3
-
pH 7.4, 37°C, Michaelis-Menten kinetic parameters
0.003
20-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
0.171
25-hydroxyvitamin D2
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
0.094
25-hydroxyvitamin D3
-
pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000002
0.00000042
-
substrate 24-oxo-25-hydroxycholecalciferol, recombinant reconstituted system
0.00000058
-
substrate 25-hydroxycholecalciferol, recombinant reconstituted system
0.0000015
0.0000072
-
purified cytochrome P-450 component of 1alpha-hydroxylase, reconstituted system
0.0000082
-
purified cytochrome P-450 component of 1alpha-hydroxylase, reconstituted system
0.602
-
reduction of cytochrome P-450 at non-saturating level of enzyme components
11.38
-
reconstituted system of cytochrome P-450, cytochrome b5, adrenocortical ferredoxin reductase, and renal ferredoxin
additional information
additional information
-
higher activity in male kidney compared to female kidney
additional information
-
1alpha-hydroxylation activity of the full-length enzyme form is 10fold higher than the activity of the truncated enzyme form
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
285537, 440101, 440102, 440103, 440104, 440105, 440108, 440109, 440110, 440111, 440113, 440121, 440123
-
-
brenda
-
-
-
brenda
-
675474, 675686, 677255, 684477, 684478, 685920, 686404, 688675, 688682, 695621, 695623, 695624, 695625, 695626, 697022, 698896, 699086, 712553, 712885, 724907, 725826
-
-
brenda
CYP27B1 knockout mice, normal development when fed a 1alpha,25-dihydroxyvitamin D replacement or a high-calcium diet
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
distributed throughout all brain regions, neurons and glial cells
brenda
-
renal distal tubular epithelial cell line. CYP27B1 gene expression is unchanged after treatement with parathyroid hormone or after high Ca2+ exposure
brenda
-
expression of 1alpha-OHase is 1.25fold higher in MCF-7 compared to MCF-10A cells. In MCF-10A cells, at least 6 splice variants are detected. Alternative splicing of 1alpha-OHase can regulate the level of active enzyme
brenda
-
renal proximal tubular epithelial cell line. CYP27B1 gene expression is elevated in response to parathyroid hormone. High Ca2+ exposure represses CYP27B1 gene expression in both dose and time-dependent fashion
brenda
-
1-OHase mRNA expression is highest in pre-menopausal women and is increased by all hormones tested. In post-menopausal osteoblasts all hormones except biochainin A and genistein increase 1-OHase mRNA expressions to less extent. In male-derived osteoblasts only dihydrotestosterone and carboxybiochainin A increase 1-OHase mRNA expression
brenda
-
high enzyme and vitamin D receptor expression level, especially in regions of lymphocyte infiltration
brenda
-
prostate cancer cell line, greatly decreased activity of 25-hydroxyvitamin D-1alpha-hydroxylase due to decreased RNA transcription
brenda
-
RT-PCR and immunohistochemic expression analysis
brenda
additional information
-
parathyroid hormone increases CYP1alpha mRNA and protein in a time-dependent manner. H2O2 inhibits parathyroid hormone-stimulated CYP1alpha protein levels and 1,25(OH)2D production in a dose dependent manner. The catalytic activity of the CYP1alpha protein may be reduced by free radical damage in CYP27B1 cells
brenda
-
enzyme expression analysis in different samples of women with and without breast cancer, no correlation with breast cancer development
brenda
the enzyme expression is reduced in breast cancer cell specimen compared to healthy breast tissue
brenda
-
intestinal cell line, both butyrate and 1alpha-25(OH)2D3 stimulate differentiation of Caco-2 cells, while 25(OH)2D3 has no impact on cell differentiation
brenda
-
healthy and malignant, high expression level, 1alpha-hydroxylase is present at equal high levels in normal colonic epithelium as in ACFs, polyps, and colorectal cancer irrespective of tumor cell differentiation
brenda
-
prostate cancer cell line, greatly decreased activity of 25-hydroxyvitamin D-1alpha-hydroxylase due to decreased RNA transcription
brenda
-
-
brenda
-
RT-PCR expression and immunohistochemic analysis, low CYP27B1 expression in the atrophic kidney, predominantly expressed in proximal tubules
brenda
-
prostate cancer cell line, greatly decreased activity of 25-hydroxyvitamin D-1alpha-hydroxylase due to decreased RNA transcription
brenda
-
epidermal growth factor does not upregulate 1alpha-OHase promoter activity in the carcinogenic prostate cells. Dysregulation of 1alpha-OHase in cancer cells may lead to the aberrant growth of prostate cancer cells
brenda
-
expression of 1alpha-hydroxylase is intimately associated with toll-like receptor, TLR, recognition of pathogens in macrophages
brenda
-
expression of 1alpha-OHase is 1.25fold higher in MCF-7 compared to MCF-10A cells. MCF-7 cells show no or marginal expression levels of splice variants
brenda
enzyme expression in secondary hyperparathyroidism
brenda
-
tissue obtained from normal prostate, benign prostatic hyperplastia or cancer, primary and cultured prostate cancer cells have greatly decreased activity of 25-hydroxyvitamin D-1alpha-hydroxylase and are therefore resistant to the tumor suppressing activity of circulating 25-hydroxyvitamin D3
brenda
-
the enzyme is up-regulated by suberoylanilide hydroxamic acid, a histone deacetylase inhibitor
brenda
-
epidermal growth factor upregulates 1alpha-OHase promoter activity in the noncarcinogenic prostate cells
brenda
additional information
-
tissue-specific expression analysis, colonic and renal vitamin D hydroxylases are regulated independently, while low dietary calcium does not affect colonic expression of vitamin D receptor, VDR, or 25-hydroxyvitamin D3 1alpha-hydroxylase, it influences their renal expression by elevating CYP27B1 expression and reducing VDR and 25-hydroxyvitamin D3 24-hydroxylase expression, overview
brenda
additional information
-
both 1alpha-hydroxylase and vitaminD receptor levels are negligible in tumor cells metastasizing to regional lymph nodes
brenda
additional information
-
altered expression of 1alpha-hydroxylase in different types of neoplasm including breast, prostate and colon cancers, autocrine/paracrine synthesis of 1,25(OH)2D3 is decreased in tumor cells and cell lines
brenda
additional information
-
25OHD action involves localized extrarenal conversion to 1,25-dihydroxyvitamin D via tissue-specific expression of the enzyme 25-hydroxyvitamin D-1alpha-hydroxylase
brenda
additional information
-
no truncated enzyme form in lung, testis, heart, or brain mitochondria
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the CYP1alpha protein is located on the inner mitochondrial membrane
brenda
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
-
mechanisms for involvement of 1alpha-hydroxylase in antimicrobial responses within different barrier tissues, overview
additional information
-
25OHD action involves localized extrarenal conversion to 1,25-dihydroxyvitamin D via tissue-specific expression of the enzyme 25-hydroxyvitamin D-1alpha-hydroxylase. Expression of 1alpha-hydroxylase is intimately associated with toll-like receptor, TLR, recognition of pathogens in macrophages
malfunction
-
Hypercalcaemia in subcutaneous fat necrosis appears to be due to abundant levels of 25-hydroxyvitamin D3-1alpha-hydroxylase in immune infiltrates associated with tissue lesions
malfunction
Malakoplakia is a rare disease characterized by the presence of nongranulomatous macrophage infiltration. Malakoplakia cells may exhibit ectopic 25-hydroxyvitamin D3 1-alpha-hydroxylase activity and cause severe hypercalcemia upon vitamin D supplementation. Therefore, such supplementation should not be given in malakoplakia patients without an actual deficiency and requires careful monitoring of serum calcium
malfunction
the ethiopathogenesis of multiple sclerosis and vitamin-D-dependent rickets type 1 is based on CYP27B1 polymorphisms. A summary of the role of polymorphisms in CYP27B1 gene in the occurrence of diseases is provided
metabolism
GIST tumor 1alpha-hydroxylase activity and vitamin D receptor expression could explain the increased levels of calcitriol and subsequent hypercalcemia
metabolism
the ethiopathogenesis of multiple sclerosis and vitamin-D-dependent rickets type 1 is based on CYP27B1 polymorphisms. A summary of the role of polymorphisms in CYP27B1 gene in the occurrence of diseases is provided
metabolism
vitamin D deficiency impair outcomes of patients with diffuse large B-cell lymphoma (DLBCL) treated with rituximab-based therapy. Extrarenal 25-hydroxyvitamin D3-1alpha-hydroxylase production and proinflammatory cytokine production by lymphoma cells are considered to play a role in the pathogenesis of hypercalcemia
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
-
x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE
52000
-
x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE
55000
additional information
additional information
-
enzyme can be reconstituted with the 3 components: cytochrome P-450D1alpha, NADPH-renodoxin reductase and renodoxin
additional information
-
kidney mitochondrial 25-hydroxyvitamin D3-1alpha-hydroxylation system consists of a renal ferredoxin reductase (flavoprotein), renal ferredoxin and cytochrome P-450
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE
additional information
-
three-dimensional structure analysis of wild-type and mutant enzymes, molecular modeling and substrate docking, overview
additional information
-
amino acid sequence comparison of full-length and truncated enzyme forms
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type Vdh and mutant Vdh-K1 in complex with substrates VD3 and 25(OH)VD3, 20 mg/ml wild-type protein in 20 mM Tris-HCl, pH 7.5, supplemented with 0-0.2% PMbetaCD for VD3 complex or 0-0.2% gammaCD for 25(OH)VD3 complex, 20 mg/ml mutant protein in 20 mM Tris-HCl, pH 7.5, supplemented with 20 mM NaCl, sitting-drop method, 20°C. Vdh-WT crystals are grown using reservoir solution containing 0.1 M BisTris, pH 7.5, 50 mM CaCl2, 40-120 mM NaCl or KCl, and 32-40% PEG 400 or PEG 550 monomethyl ether or 20% PEG 1000, Vdh-K1 is crystallized using reservoir solution containing 0.1 M calcium acetate and 10-14% PEG 3350, X-ray diffraction structure determination and analysis at 1.75-3.05 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q65A
-
site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme
Q65E
-
site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme
Q65H
-
site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme
Q65L
-
site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme
Q65N
-
site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme
S408A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme
S408I
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme
S408T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme
S408V
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme
T70R/V156L/E216M/E384R
-
mutant Vdh-K1, 22fold more active in the hydroxylation of VD3 to 25(OH)VD3 than wild-type Vdh in in vivo bioconversion using Escherichia coli cells. backbone and side chain conformations at the active-site pocket are identical among the substrate-free, VD3-bound, and 25(OH)VD3-bound forms of Vdh-K1, and no induced-fit mechanisms are observed, although VD3 is asymmetric
additional information
additional information
-
expression of vitamin D hydroxylases in the VDR-/- mouse model, overview
additional information
-
construction of a transgenic mouse line expressing 1501 bp of 58 flanking region together with 44 bp of 58 untranslated region of the human CYP27B1 gene fused to the firefly luciferase reporter gene, luciferase protein and mRNA for CYP27B1 are localized to proximal convoluted tubule cells of the kidney with highest levels in 2-week-old animals, overview
additional information
construction and expression in COS cell line of a chimeric fusion protein: vitaminD receptor ligand-binding domain with the yeast GAL4 DNA-binding domain, also expression of lacZ containing reporter plasmid
additional information
-
construction of 25-hydroxyvitamin D-1alpha-hydroxylase and PTH double knockout mice, NH2-terminal fragments of PTH and PTH-related protein, PTHrP, on the skeleton of young mutant mice is an increase in both endochondral bone and appositional formation without increased bone resorption, phenotype, overview, PTH is the major protein hormone regulating calcium homeostasis, PTHrP is a PTH-like factor responsible for humoral hypercalcemia of malignancy, both peptides are required to achieve normal fetal skeletal morphogenesis
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CYP27B1 is labile during purification despite the presence of 20% glycerol as a stabilizing agent
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, prolonged standing of the enzyme, including overnight dialysis, causes marked loss of the holo-enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged CYP27B1 from Escherichia coli strain JM109 by nickel affinity chromatoghraphy, followed by affinity chromatography on a bovine adrenodoxin-coupled resin with elution by 1.0% CHAPS
-
recombinant wild-type Vdh and mutant Vdh-K1 from Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of several novel intron 2-containing, noncoding splice variant mRNAs for CYP27b1 in 1,25(OH)2D3-producing HKC-8 human proximal tubule and THP-1 monocytic cells. Noncoding splice variants of CYP27b1 are functionally active and may play a significant role in the regulation of 1,25(OH)2D3 synthesis during normal physiology
-
expression in COS cells, reconstituted with recombinant cytochrome P-450, recombinant adrenodoxin, and recombinant adrenodoxin reductase
expression in COS cells, vitamin D3 25- and 1alpha-hydroxylase, DNA sequence analysis
-
expression in Escherichia coli JM109, coexpression of adrenodoxin and NADPH-adrenodoxin reductase for reconstitution of the system
-
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
expression of wild-type Vdh and mutant Vdh-K1 in Escherichia coli
-
His-tag, expressed in Rhodococcus erythropolis and Escherichia coli
-
quantitative PCR analysis of gene expression in different tissues/cells, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
calcitonin induces 25-hydroxyvitamin D3 1alpha-hydroxylase protein levels in AOK-B50 cells transfected with a mouse 25-hydroxyvitamin D3 1alpha-hydroxylase promoter construct (transcription factor C/EBPbeta is involved)
-
expression of 1alpha-hydroxylase is induced via toll-like receptor, TLR, recognition of pathogens in macrophages, but not in colonic cells, i.e. Caco-2 and BBe colonic cell lines. Colonic epithelial cells may require specific factors to initiate intracrine responses to vitamin D.
-
fibroblast growth factor 23 (FGF 23) inhibits 1alpha(OH)ase expression via MAPK/ERK
genes CYP2R1 encoding vitamin D 25-hydroxylase, CYP27B1 encoding 25-hydroxyvitamin D-1 alpha hydroxylase and CYP24A1 encoding 1,25-dihydroxyvitamin D(3) 24-hydroxylase are upregulated in clear cell renal cell carcinomas compared with normal tissue. CYP24A1 displays a significantly higher expression in tumors than CYP27B1 and CYP2R1, whereas no differences in the expression of these genes are found in healthy renal tissue
-
hyperplastic parathyroid glands from patients with chronic kidney failure normally display a heterogeneous cellularity. 25-hydroxyvitamin D3 1alpha-hydroxylase is expressed at much higher levels in oxyphil cells than in chief cells in these patients. The calcimimetic cinacalcet increases the expression of the enzyme in human parathyroid cultures
-
kidney: 25-hydroxycholecalciferol induces a significant downregulation 3 days after injection
kidney: calcitriol and 25-hydroxycholecalciferol induce a significant upregulation 6 days after injection
kidney: parathyroid hormone-related protein induces significant upregulation 6 h after injection
parathyroid hormone (PTH) increases the protein level of 1alpha(OH)ase in human epidermal keratinocyte cell line HaCaT
statistically significantly lower protein expression in malignant ovarian tissue
-
sterol regulatory element binding protein 1 (SREBP1) is activates CYP27B1 transcription
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
genes CYP2R1 encoding vitamin D 25-hydroxylase, CYP27B1 encoding 25-hydroxyvitamin D-1 alpha hydroxylase and CYP24A1 encoding 1,25-dihydroxyvitamin D(3) 24-hydroxylase are upregulated in clear cell renal cell carcinomas compared with normal tissue. CYP24A1 displays a significantly higher expression in tumors than CYP27B1 and CYP2R1, whereas no differences in the expression of these genes are found in healthy renal tissue. Gene expression of CYP2R1, CYP27B1 and CYP24A does not differ between pathological classifications
medicine
-
hyperplastic parathyroid glands from patients with chronic kidney failure normally display a heterogeneous cellularity. 25-hydroxyvitamin D3 1alpha-hydroxylase is expressed at much higher levels in oxyphil cells than in chief cells in these patients. The calcimimetic cinacalcet increases the expression of the enzyme in human parathyroid cultures. The enzyme in human parathyroid cultures is functionally active
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoon, P.S.; DeLuca, H.F.
Purification and properties of vitamin D hydroxylases
Methods Enzymol.
67
430-440
1980
Gallus gallus
brenda
Gray, R.W.; Omdahl, J.L.; Ghazarian, J.G.; DeLuca, H.F.
25-Hydroxycholecalciferol-1-hydroxylase. Subcellular location and properties
J. Biol. Chem.
247
7528-7532
1972
Gallus gallus
brenda
Botham, K.M.; Tanaka, Y.; DeLuca, H.F.
25-Hydroxyvitamin D3-1-hydroxylase. Inhibition in vitro by rat and pig tissues
Biochemistry
13
4961-4966
1974
Gallus gallus
brenda
Ghazarian, J.G.; Kream, B.; Botham, K.M.; Nickells, M.W.; DeLuca, H.F.
Rat plasma 25-hydroxyvitamin D3 binding protein: an inhibitor of the 25-hydroxyvitamin D3-1alpha-hydroxylase
Arch. Biochem. Biophys.
189
212-220
1978
Gallus gallus
brenda
Henry, H.L.; Norman, A.W.
Studies on calciferol metabolism. Regulation of 25-hydroxyvitamin D3-1-hydroxylase in isolated renal mitochondria
Arch. Biochem. Biophys.
172
582-589
1976
Gallus gallus
brenda
Botham, K.M.; Ghazarian, J.G.; Kream, B.E.; DeLuca, H.F.
Isolation of an inhibitor of 25-hydroxyvitamin D3-1-hydroxylase from rat serum
Biochemistry
15
2130-2135
1976
Gallus gallus
brenda
Paulson, S.K.; DeLuca, H.F.
Subcellular location and properties of rat renal 25-hydroxyvitamin D3-1 alpha-hydroxylase
J. Biol. Chem.
260
11488-11492
1985
Rattus norvegicus
brenda
Vieth, R.; Fraser, D.
Kinetic behavior of 25-hydroxyvitamin D-1-hydroxylase and -24-hydroxylase in rat kidney mitochondria
J. Biol. Chem.
254
12455-12460
1979
Rattus norvegicus
brenda
Ghazarian, J.G.; Yanda, D.M.
Inhibition of 25-hydroxyvitamin D 1 alpha-hydroxylase by renal mitochondrial protein kinase-catalyzed phosphorylation
Biochem. Biophys. Res. Commun.
132
1095-1102
1985
Gallus gallus
brenda
Ghazarian, J.G.; Jefcoate, C.R.; Knutson, J.C.; Orme-Johnson, W.H.; DeLuca, H.F.
Mitochondrial cytochrome P450. A component of chick kidney 25-hydrocholecalciferol-1alpha-hydroxylase
J. Biol. Chem.
249
3026-3033
1974
Gallus gallus
brenda
Henry, H.L.; Norman, A.W.
Studies on calciferol metabolism. IX. Renal 25-hydroxy-vitamin D3-1 hydroxylase. Involvement of cytochrome P-450 and other properties
J. Biol. Chem.
249
7529-7535
1974
Gallus gallus
brenda
Kulkoski, J.A.; Ghazarian, J.G.
Purification and characterization of the ferredoxin component of 25-hydroxycholecalciferol 1 alpha-hydroxylase
Biochem. J.
177
673-678
1979
Gallus gallus
brenda
Gray, R.W.; Ghazarian, J.G.
Solubilization and reconstitution of kidney 25-hydroxyvitamin D3 1 alpha- and 24-hydroxylases from vitamin D-replete pigs
Biochem. J.
259
561-568
1989
Sus scrofa
brenda
Pedersen, J.I.; Ghazarian, J.G.; Orme-Johnson, N.R.; DeLuca, H.F.
Isolation of chick renal mitochondrial ferredoxin active in the 25-hydroxyvitamin D3-1alpha-hydroxylase system
J. Biol. Chem.
251
3933-3941
1976
Gallus gallus
brenda
Postlind, H.
Separation of the cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3
Biochem. Biophys. Res. Commun.
168
261-266
1990
Sus scrofa
brenda
Hiwatashi, A.; Nishii, Y.; Ichikawa, Y.
Purification of cytochrome P-450D1 alpha (25-hydroxyvitamin D3-1 alpha-hydroxylase) of bovine kidney mitochondria
Biochem. Biophys. Res. Commun.
105
320-327
1982
Bos taurus
brenda
Hagenfeldt, Y.; Pedersen, J.I.; Bjrkhem, I.
Properties of guinea-pig kidney 25-hydroxyvitamin D3 1 alpha-hydroxylase assayed by isotope dilution-mass spectrometry
Biochem. J.
250
521-526
1988
Cavia porcellus
brenda
Paulson, S.K.; Phelps, M.; DeLuca, H.F.
Assay and properties of rat yolk sac 25-hydroxyvitamin D3 1 alpha-hydroxylase
Biochemistry
25
6821-6826
1986
Rattus norvegicus
brenda
Lobaugh, B.; Almond, J.R.; Drezner, M.K.
Measurement of 25-hydroxyvitamin D 1-alpha-hydroxylase activity in mammalian kidney
Methods Enzymol.
123
159-167
1986
Mammalia
brenda
Delvin, E.E.; Arabian, A.
Kinetics and regulation of 25-hydroxycholecalciferol 1 alpha-hydroxylase from cells isolated from human term decidua
Eur. J. Biochem.
163
659-662
1987
Homo sapiens
brenda
Burgos-Trinidad, M.; Ismail, R.; Ettinger, R.A.; Prahl, J.M.; DeLuca, H.F.
Immunopurified 25-hydroxyvitamin D 1a-hydroxylase and 1,25-dihydroxyvitamin D 24-hydroxylase are closely related but distinct enzymes
J. Biol. Chem.
267
3498-3505
1992
Gallus gallus
brenda
Grieff, M.; Dusso, A.; Mori, T.; Nishii, Y.; Slatopolsky, E.; Brown, A.J.
22-Oxacalcitriol suppresses 25-hydroxycholecalciferol-1a-hydroxylase in rat kidney
Biochem. Biophys. Res. Commun.
185
191-196
1992
Rattus norvegicus
brenda
Daniel, D.; Middleton, R.; Henry, H.L.; Okamura, W.H.
Inhibitors of 25-hydroxyvitamin D3 1a-hydroxylase: A-ring oxa analogs of 25-hydroxyvitamin D3
J. Org. Chem.
61
5617-5625
1996
Gallus gallus
-
brenda
Nakamura, Y.; Eto, T.A.; Taniguchi, T.; Miyamoto, K.; Nagatomo, J.; Shiotsuki, H.; Sueta, H.; Higashi, S.; Okuda, K.I.; Setoguchi, T.
Purification and characterization of 25-hydroxyvitamin D3 1alpha-hydroxylase from rat kidney mitochondria
FEBS Lett.
419
45-48
1997
Rattus norvegicus
brenda
Takeyama, K.i.; Kitanaka, S.; Sato, T.; Kobori, M.; Yanagisawa, J.; Kato, S.
25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis
Science
277
1827-1830
1997
Mus musculus (O35084)
brenda
Sawada, N.; Sakaki, T.; Kitanaka, S.; Takeyama, K.i.; Kato, S.; Inouye, K.
Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase: coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli
Eur. J. Biochem.
265
950-956
1999
Homo sapiens
brenda
Sakaki, T.; Sawada, N.; Takeyama, K.i.; Kato, S.; Inouye, K.
Enzymic properties of mouse 25-hydroxyvitamin D3 1alpha-hydroxylase expressed in Escherichia coli
Eur. J. Biochem.
259
731-738
1999
Mus musculus
brenda
Yoshida, T.; Yoshida, N.; Nakamura, A.; Monkawa, T.; Hayashi, M.; Saruta, T.
Cloning of porcine 25-hydroxyvitamin D3 1alpha-hydroxylase and its regulation by cAMP in LLC-PK1 cells
J. Am. Soc. Nephrol.
10
963-970
1999
Sus scrofa (Q9XS57), Sus scrofa
brenda
Hagenfeldt, Y.; Berlin, T.
The human renal 25-hydroxyvitamin D3-1a-hydroxylase: properties studied by isotope-dilution mass spectrometry
Eur. J. Clin. Invest.
22
223-228
1992
Homo sapiens
brenda
Bareis, P.; Kallay, E.; Bischof, M.G.; Bises, G.; Hofer, H.; Potzi, C.; Manhardt, T.; Bland, R.; Cross, H.S.
Clonal differences in expression of 25-hydroxyvitamin D(3)-1alpha-hydroxylase, of 25-hydroxyvitamin D(3)-24-hydroxylase, and of the vitamin D receptor in human colon carcinoma cells: effects of epidermal growth factor and 1alpha,25-dihydroxyvitamin D(3)
Exp. Cell Res.
276
320-327
2002
Homo sapiens
brenda
Inouye, K.; Sakaki, T.
Enzymatic studies on the key enzymes of vitamin D metabolism; 1alpha-hydroxylase (CYP27B1) and 24-hydroxylase (CYP24)
Biotechnol. Annu. Rev.
7
179-194
2001
Homo sapiens, Mus musculus
brenda
Diaz, L.; Arranz, C.; Avila, E.; Halhali, A.; Vilchis, F.; Larrea, F.
Expression and activity of 25-hydroxyvitamin D-1alpha-hydroxylase are restricted in cultures of human syncytiotrophoblast cells from preeclamptic pregnancies
J. Clin. Endocrinol. Metab.
87
3876-3882
2002
Homo sapiens
brenda
Hosseinpour, F.; Norlin, M.; Wikvall, K.
Kidney microsomal 25- and 1alpha-hydroxylase in vitamin D metabolism: catalytic properties, molecular cloning, cellular localization and expression during development
Biochim. Biophys. Acta
1580
133-144
2002
Sus scrofa
brenda
Somjen, D.; Weisman, Y.; Kohen, F.; Gayer, B.; Limor, R.; Sharon, O.; Jaccard, N.; Knoll, E.; Stern, N.
25-Hydroxyvitamin D3-1alpha-hydroxylase is expressed in human vascular smooth muscle cells and is upregulated by parathyroid hormone and estrogenic compounds
Circulation
111
1666-1671
2005
Homo sapiens
brenda
Panda, D.K.; Miao, D.; Bolivar, I.; Li, J.; Huo, R.; Hendy, G.N.; Goltzman, D.
Inactivation of the 25-hydroxyvitamin D 1alpha-hydroxylase and vitamin D receptor demonstrates independent and interdependent effects of calcium and vitamin D on skeletal and mineral homeostasis
J. Biol. Chem.
279
16754-16766
2004
Mus musculus
brenda
St-Arnaud, R.; Dardenne, O.; Prud'homme, J.; Hacking, S.A.; Glorieux, F.H.
Conventional and tissue-specific inactivation of the 25-hydroxyvitamin D-1alpha-hydroxylase (CYP27B1)
J. Cell. Biochem.
88
245-251
2003
Mus musculus
brenda
Eyles, D.W.; Smith, S.; Kinobe, R.; Hewison, M.; McGrath, J.J.
Distribution of the vitamin D receptor and 1alpha-hydroxylase in human brain
J. Chem. Neuroanat.
29
21-30
2005
Homo sapiens
brenda
Diesel, B.; Seifert, M.; Radermacher, J.; Fischer, U.; Tilgen, W.; Reichrath, J.; Meese, E.
Towards a complete picture of splice variants of the gene for 25-hydroxyvitamin D3 1alpha-hydroxylase in brain and skin cancer
J. Steroid Biochem. Mol. Biol.
89-90
527-532
2004
Homo sapiens
brenda
Khorchide, M.; Lechner, D.; Cross, H.S.
Epigenetic regulation of vitamin D hydroxylase expression and activity in normal and malignant human prostate cells
J. Steroid Biochem. Mol. Biol.
93
167-172
2005
Homo sapiens
brenda
Ma, J.F.; Nonn, L.; Campbell, M.J.; Hewison, M.; Feldman, D.; Peehl, D.M.
Mechanisms of decreased Vitamin D 1alpha-hydroxylase activity in prostate cancer cells
Mol. Cell. Endocrinol.
221
67-74
2004
Homo sapiens
brenda
Friedrich, M.; Diesing, D.; Cordes, T.; Fischer, D.; Becker, S.; Chen, T.C.; Flanagan, J.N.; Tangpricha, V.; Gherson, I.; Holick, M.F.; Reichrath, J.
Analysis of 25-hydroxyvitamin D3-1alpha-hydroxylase in normal and malignant breast tissue
Anticancer Res.
26
2615-2620
2006
Homo sapiens
brenda
Furster, C.; Bergman, T.; Wikvall, K.
Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria
Biochem. Biophys. Res. Commun.
263
663-666
1999
Oryctolagus cuniculus
brenda
Segersten, U.; Holm, P.K.; Bjrklund, P.; Hessman, O.; Nordgren, H.; Binderup, L.; Akerstrm, G.; Hellman, P.; Westin, G.
25-Hydroxyvitamin D3 1alpha-hydroxylase expression in breast cancer and use of non-1alpha-hydroxylated vitamin D analogue
Breast Cancer Res.
7
R980-R986
2005
Homo sapiens (O15528)
brenda
Matusiak, D.; Murillo, G.; Carroll, R.E.; Mehta, R.G.; Benya, R.V.
Expression of vitamin D receptor and 25-hydroxyvitamin D3-1{alpha}-hydroxylase in normal and malignant human colon
Cancer Epidemiol. Biomarkers Prev.
14
2370-2376
2005
Homo sapiens
brenda
Kallay, E.; Bises, G.; Bajna, E.; Bieglmayer, C.; Gerdenitsch, W.; Steffan, I.; Kato, S.; Armbrecht, H.J.; Cross, H.S.
Colon-specific regulation of vitamin D hydroxylases - a possible approach for tumor prevention
Carcinogenesis
26
1581-1589
2005
Homo sapiens
brenda
Yamamoto, K.; Uchida, E.; Urushino, N.; Sakaki, T.; Kagawa, N.; Sawada, N.; Kamakura, M.; Kato, S.; Inouye, K.; Yamada, S.
Identification of the amino acid residue of CYP27B1 responsible for binding of 25-hydroxyvitamin D3 whose mutation causes vitamin D-dependent rickets type 1
J. Biol. Chem.
280
30511-30516
2005
Mus musculus
brenda
Xue, Y.; Zhang, Z.; Karaplis, A.C.; Hendy, G.N.; Goltzman, D.; Miao, D.
Exogenous PTH-related protein and PTH improve mineral and skeletal status in 25-hydroxyvitamin D-1alpha-hydroxylase and PTH double knockout mice
J. Bone Miner. Res.
20
1766-1777
2005
Mus musculus
brenda
Stoffels, K.; Overbergh, L.; Giulietti, A.; Verlinden, L.; Bouillon, R.; Mathieu, C.
Immune regulation of 25-hydroxyvitamin-D3-1alpha-hydroxylase in human monocytes
J. Bone Miner. Res.
21
37-47
2006
Homo sapiens
brenda
Overbergh, L.; Stoffels, K.; Waer, M.; Verstuyf, A.; Bouillon, R.; Mathieu, C.
Immune regulation of 25-hydroxyvitamin D-1alpha-hydroxylase in human monocytic THP1 cells: mechanisms of interferon-gamma-mediated induction
J. Clin. Endocrinol. Metab.
91
3566-3574
2006
Homo sapiens (O15528), Homo sapiens
brenda
Khadzkou, K.; Buchwald, P.; Westin, G.; Dralle, H.; Akerstroem, G.; Hellman, P.
25-hydroxyvitamin D3 1alpha-hydroxylase and vitamin D receptor expression in papillary thyroid carcinoma
J. Histochem. Cytochem.
54
355-361
2006
Homo sapiens
brenda
Hendrix, I.; Anderson, P.H.; Omdahl, J.L.; May, B.K.; Morris, H.A.
Response of the 5-flanking region of the human 25-hydroxyvitamin D 1alpha-hydroxylase gene to physiological stimuli using a transgenic mouse model
J. Mol. Endocrinol.
34
237-245
2005
Homo sapiens
brenda
Carneiro de Lyra, E.; Amorim da Silva, I.; Katayama, M.L.; Brentani, M.M.; Nonogaki, S.; Goes, J.C.; Folgueira, M.A.
25(OH)D3 and 1,25(OH)2D3 serum concentration and breast tissue expression of 1alpha-hydroxylase, 24-hydroxylase and Vitamin D receptor in women with and without breast cancer
J. Steroid Biochem. Mol. Biol.
100
184-192
2006
Homo sapiens
brenda
Townsend, K.; Evans, K.N.; Campbell, M.J.; Colston, K.W.; Adams, J.S.; Hewison, M.
Biological actions of extra-renal 25-hydroxyvitamin D-1alpha-hydroxylase and implications for chemoprevention and treatment
J. Steroid Biochem. Mol. Biol.
97
103-109
2005
Homo sapiens
brenda
Schroeder, O.; Turak, S.; Daniel, C.; Gaschott, T.; Stein, J.
Upregulation of 25-hydroxyvitamin D3-1alpha-hydroxylase by butyrate in Caco-2 cells
World J. Gastroenterol.
11
7136-7141
2005
Homo sapiens
brenda
Wang, L.; Persons, K.S.; Jamieson, D.; Flanagan, J.N.; Hsu, H.H.; Holick, M.F.; Luo, Z.; Sakaki, T.; Urushino, N.; Faller, D.V.; Chen, T.C.
Prostate 25-hydroxyvitamin D-1alpha-hydroxylase is up-regulated by suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor
Anticancer Res.
28
2009-2013
2008
Homo sapiens
brenda
Chen, T.C.
25-Hydroxyvitamin D-1 alpha-hydroxylase (CYP27B1) is a new class of tumor suppressor in the prostate
Anticancer Res.
28
2015-2017
2008
Homo sapiens
brenda
Bajwa, A.; Forster, M.N.; Maiti, A.; Woolbright, B.L.; Beckman, M.J.
Specific regulation of CYP27B1 and VDR in proximal versus distal renal cells
Arch. Biochem. Biophys.
477
33-42
2008
Mus musculus
brenda
Fischer, D.; Seifert, M.; Becker, S.; Ludders, D.; Cordes, T.; Reichrath, J.; Friedrich, M.
25-Hydroxyvitamin D3 1alpha-hydroxylase splice variants in breast cell lines MCF-7 and MCF-10
Cancer Genomics Proteomics
4
295-300
2007
Homo sapiens
brenda
Urushino, N.; Nakabayashi, S.; Arai, M.A.; Kittaka, A.; Chen, T.C.; Yamamoto, K.; Hayashi, K.; Kato, S.; Ohta, M.; Kamakura, M.; Ikushiro, S.; Sakaki, T.
Kinetic studies of 25-hydroxy-19-nor-vitamin D3 and 1alpha,25-dihydroxy-19-nor-vitamin D3 hydroxylation by CYP27B1 and CYP24A1
Drug Metab. Dispos.
35
1482-1488
2007
Mus musculus
brenda
Wu, S.; Ren, S.; Nguyen, L.; Adams, J.S.; Hewison, M.
Splice variants of the CYP27b1 gene and the regulation of 1,25-dihydroxyvitamin D3 production
Endocrinology
148
3410-3418
2007
Homo sapiens
brenda
Hewison, M.; Burke, F.; Evans, K.N.; Lammas, D.A.; Sansom, D.M.; Liu, P.; Modlin, R.L.; Adams, J.S.
Extra-renal 25-hydroxyvitamin D3-1alpha-hydroxylase in human health and disease
J. Steroid Biochem. Mol. Biol.
103
316-321
2007
Homo sapiens
brenda
Armbrecht, H.J.; Boltz, M.A.; Ritter, C.S.; Brown, A.J.
Parathyroid hormone stimulation of the renal 25-hydroxyvitamin D-1alpha-hydroxylase-effect of age and free radicals
J. Steroid Biochem. Mol. Biol.
103
330-333
2007
Sus scrofa
brenda
Somjen, D.; Katzburg, S.; Stern, N.; Kohen, F.; Sharon, O.; Limor, R.; Jaccard, N.; Hendel, D.; Weisman, Y.
25 hydroxy-vitamin D(3)-1alpha hydroxylase expression and activity in cultured human osteoblasts and their modulation by parathyroid hormone, estrogenic compounds and dihydrotestosterone
J. Steroid Biochem. Mol. Biol.
107
238-244
2007
Homo sapiens
brenda
Yasutake, Y.; Fujii, Y.; Cheon, W.K.; Arisawa, A.; Tamura, T.
Crystallization and preliminary X-ray diffraction studies of vitamin D3 hydroxylase, a novel cytochrome P450 isolated from Pseudonocardia autotrophica
Acta Crystallogr. Sect. F
65
372-375
2009
Pseudonocardia autotrophica
brenda
McCarthy, K.; Laban, C.; Bustin, S.A.; Ogunkolade, W.; Khalaf, S.; Carpenter, R.; Jenkins, P.J.
Expression of 25-hydroxyvitamin D-1-alpha-hydroxylase, and vitamin D receptor mRNA in normal and malignant breast tissue
Anticancer Res.
29
155-157
2009
Homo sapiens
brenda
Fischer, D.; Thome, M.; Becker, S.; Cordes, T.; Diedrich, K.; Friedrich, M.; Thill, M.
25-Hydroxyvitamin D3 1alpha-hydroxylase splice variants in benign and malignant ovarian cell lines and tissue
Anticancer Res.
29
3627-3633
2009
Homo sapiens
brenda
Fischer, D.; Becker, S.; Cordes, T.; Buecker, B.; Diedrich, K.; Friedrich, M.; Salehin, D.; Thill, M.
Vitamin D-24-hydroxylase in benign and malignant breast tissue and cell lines
Anticancer Res.
29
3641-3645
2009
Homo sapiens
brenda
Seifert, M.; Tilgen, W.; Reichrath, J.
Expression of 25-hydroxyvitamin D-1alpha-hydroxylase (1alphaOHase, CYP27B1) splice variants in HaCaT keratinocytes and other skin cells: modulation by culture conditions and UV-B treatment in vitro
Anticancer Res.
29
3659-3667
2009
Homo sapiens
brenda
Cross, H.S.; Nittke, T.; Peterlik, M.
Modulation of vitamin D synthesis and catabolism in colorectal mucosa: a new target for cancer prevention
Anticancer Res.
29
3705-3712
2009
Homo sapiens
brenda
Farooque, A.; Moss, C.; Zehnder, D.; Hewison, M.; Shaw, N.J.
Expression of 25-hydroxyvitamin D3-1alpha-hydroxylase in subcutaneous fat necrosis
Br. J. Dermatol.
160
423-425
2009
Homo sapiens
brenda
Zhong, Y.; Armbrecht, H.J.; Christakos, S.
Calcitonin, a regulator of the 25-hydroxyvitamin D3 1alpha-hydroxylase gene
J. Biol. Chem.
284
11059-11069
2009
Sus scrofa
brenda
Novakovic, B.; Sibson, M.; Ng, H.K.; Manuelpillai, U.; Rakyan, V.; Down, T.; Beck, S.; Fournier, T.; Evain-Brion, D.; Dimitriadis, E.; Craig, J.M.; Morley, R.; Saffery, R.
Placenta-specific methylation of the vitamin D 24-hydroxylase gene: implications for feedback autoregulation of active vitamin D levels at the fetomaternal interface
J. Biol. Chem.
284
14838-14848
2009
Homo sapiens
brenda
Lauter, K.; Arnold, A.
Analysis of CYP27B1, encoding 25-hydroxyvitamin D-1alpha-hydroxylase, as a candidate tumor suppressor gene in primary and severe secondary/tertiary hyperparathyroidism
J. Bone Miner. Res.
24
102-104
2009
Homo sapiens
brenda
St-Arnaud, R.; Arabian, A.; Yu, V.W.; Akhouayri, O.; Knutson, J.C.; Strugnell, S.A.
1alpha,24(S)(OH)2D2 normalizes bone morphology and serum parathyroid hormone without hypercalcemia in 25-hydroxyvitamin D-1-hydroxylase (CYP27B1)-deficient mice, an animal model of vitamin D deficiency with secondary hyperparathyroidism
J. Endocrinol. Invest.
31
711-717
2008
Mus musculus
brenda
Bevelander, G.S.; Pinto, E.S.; Canario, A.V.; Spanings, T.; Flik, G.
CYP27A1 expression in gilthead sea bream (Sparus auratus, L.): effects of calcitriol and parathyroid hormone-related protein
J. Endocrinol.
196
625-635
2008
Sparus aurata (B0BCH8)
brenda
Li, J.; Byrne, M.E.; Chang, E.; Jiang, Y.; Donkin, S.S.; Buhman, K.K.; Burgess, J.R.; Teegarden, D.
1alpha,25-Dihydroxyvitamin D hydroxylase in adipocytes
J. Steroid Biochem. Mol. Biol.
112
122-126
2008
Rattus norvegicus
brenda
Ohnishi, M.; Nakatani, T.; Lanske, B.; Razzaque, M.S.
Reversal of mineral ion homeostasis and soft-tissue calcification of klotho knockout mice by deletion of vitamin D 1alpha-hydroxylase
Kidney Int.
75
1166-1172
2009
Mus musculus
brenda
Yasutake, Y.; Fujii, Y.; Nishioka, T.; Cheon, W.K.; Arisawa, A.; Tamura, T.
Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
J. Biol. Chem.
285
31193-31201
2010
Pseudonocardia autotrophica
brenda
Dhawan, P.; Christakos, S.
Novel regulation of 25-hydroxyvitamin D3 24-hydroxylase (24(OH)ase) transcription by glucocorticoids: cooperative effects of the glucocorticoid receptor, C/EBP beta, and the vitamin D receptor in 24(OH)ase transcription
J. Cell. Biochem.
110
1314-1323
2010
Homo sapiens
brenda
Tang, E.K.; Voo, K.J.; Nguyen, M.N.; Tuckey, R.C.
Metabolism of substrates incorporated into phospholipid vesicles by mouse 25-hydroxyvitamin D3 1alpha-hydroxylase (CYP27B1)
J. Steroid Biochem. Mol. Biol.
119
171-179
2010
Mus musculus
brenda
Lagishetty, V.; Chun, R.F.; Liu, N.Q.; Lisse, T.S.; Adams, J.S.; Hewison, M.
1alpha-hydroxylase and innate immune responses to 25-hydroxyvitamin D in colonic cell lines
J. Steroid Biochem. Mol. Biol.
121
228-233
2010
Homo sapiens
brenda
Urbschat, A.; Paulus, P.; von Quernheim, Q.F.; Brueck, P.; Badenhoop, K.; Zeuzem, S.; Ramos-Lopez, E.
Vitamin D hydroxylases CYP2R1, CYP27B1 and CYP24A1 in renal cell carcinoma
Eur. J. Clin. Invest.
43
1282-1290
2013
Homo sapiens
brenda
Ritter, C.S.; Haughey, B.H.; Armbrecht, H.J.; Brown, A.J.
Distribution and regulation of the 25-hydroxyvitamin D3 1alpha-hydroxylase in human parathyroid glands
J. Steroid Biochem. Mol. Biol.
130
73-80
2012
Homo sapiens
brenda
Chun, R.F.; Blatter, E.; Elliott, S.; Fitz-Gibbon, S.; Rieger, S.; Sagasti, A.; Adams, J.S.; Hewison, M.
Cloning of a functional 25-hydroxyvitamin D-1alpha-hydroxylase in zebrafish (Danio rerio)
Cell Biochem. Funct.
32
675-682
2014
Danio rerio (A0A097HUX0), Danio rerio
brenda
Kagawa, T.; Kozai, M.; Masuda, M.; Harada, N.; Nakahashi, O.; Tajiri, M.; Yoshikawa, R.; Nakao, M.; Takei, Y.; Iwano, M.; Takeda, E.; Taketani, Y.; Yamamoto, H.
Sterol regulatory element binding protein 1 trans-activates 25-hydroxy vitamin D3 24-hydroxylase gene expression in renal proximal tubular cells
Biochem. Biophys. Res. Commun.
500
275-282
2018
Homo sapiens (O15528)
brenda
Nakayama, S.; Matsuda, M.
25-Hydroxyvitamin D3-1alpha-hydroxylase - and multiple cytokine-producing diffuse large B-cell lymphoma
Blood
131
2271
2018
Homo sapiens (O15528)
brenda
Wu, W.; Fan, H.; Jiang, Y.; Liao, L.; Li, L.; Zhao, J.; Zhang, H.; Shrestha, C.; Xie, Z.
Regulation of 25-hydroxyvitamin D-1-hydroxylase and 24-hydroxylase in keratinocytes by PTH and FGF23
Exp. Dermatol.
27
1201-1209
2018
Homo sapiens (O15528)
brenda
Herrera-Martinez, Y.; Contreras Gonzalez, M.J.; Pedraza-Arevalo, S.; Guerrero Martinez, M.D.C.; Rodrigo Martinez, A.; Gonzalez Menchen, A.; Blanco Molina, M.A.; Galvez-Moreno, M.A.; Moreno-Vega, A.L.; Luque, R.M.; Herrera-Martinez, A.D.
Calcitriol-mediated hypercalcemia, somatostatin receptors expression and 25-hydroxyvitamin D3-1alpha-hydroxylase in GIST tumors
Front. Endocrinol. (Lausanne)
12
812385
2021
Homo sapiens (O15528)
brenda
Chemouny, J.M.; Sannier, A.; Hanouna, G.; Champion, L.; Vrtovsnik, F.; Daugas, E.
Malakoplakia as a cause of severe hypercalcemia through ectopic 25-hydroxyvitamin D3 1-alpha-hydroxylase expression A case report
Medicine (Baltimore)
97
e12090
2018
Homo sapiens (O15528)
brenda
Latacz, M.; Snarska, J.; Kostyra, E.; Fiedorowicz, E.; Savelkoul, H.F.; Grzybowski, R.; Cieslinska, A.
Single nucleotide polymorphisms in 25-hydroxyvitamin D3 1-alpha-hydroxylase (CYP27B1) gene the risk of malignant tumors and other chronic diseases
Nutrients
12
801
2020
Homo sapiens (O15528)
brenda
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