Information on EC 1.14.99.38 - cholesterol 25-hydroxylase and Organism(s) Homo sapiens and UniProt Accession P08684

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Homo sapiens
UNIPROT: P08684
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The expected taxonomic range for this enzyme is: Tetrapoda


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
1.14.99.38
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RECOMMENDED NAME
GeneOntology No.
cholesterol 25-hydroxylase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Primary bile acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
cholesterol,hydrogen-donor:oxygen oxidoreductase (25-hydroxylating)
Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P-450. Instead, it uses diiron cofactors to catalyse the hydroxylation of hydrophobic substrates [1]. The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues [4,5]. In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs).
CAS REGISTRY NUMBER
COMMENTARY hide
60202-07-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Ch25h
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
patients with hereditary spastic paresis, a rare inherited disease with mutations in the CYP7B1 gene, have highly elevated levels of 25- and 27-hydroxycholesterol but normal levels of cholesterol and bile acids
physiological function
additional information
the high concentrations of vitamin D3 metabolites required for upregulation of the cholesterol 25-hydroxylase gene makes it unlikely that these metabolites are important regulators of cholesterol 25-hydroxylase in vivo
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cholesterol + AH2 + O2
25-hydroxycholesterol + A + H2O
show the reaction diagram
cholesterol + AH2 + O2
25-hydroxycholesterol + A + H2O
show the reaction diagram
additional information
?
-
25-hydroxycholesterol is a secondary autoxidation product derived from 3beta-hydroxy-cholest-5-ene-25-hydroperoxide, a hydroperoxide identified in air-aged cholesterol. Thermal decomposition of 3beta-hydroxy-cholest-5-ene-25-hydroperoxide gives rise to 25-hydroxycholesterol
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cholesterol + AH2 + O2
25-hydroxycholesterol + A + H2O
show the reaction diagram
P05177, P08684, P10635, P11712
production of 25-hydroxycholesterol by intact CYP3A4, most significant activity is 25-hydroxylation, which is higher than that of 4beta-hydroxylation, a marker activity of CYP3A4
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-
?
cholesterol + AH2 + O2
25-hydroxycholesterol + A + H2O
show the reaction diagram
additional information
?
-
Q02318
25-hydroxycholesterol is a secondary autoxidation product derived from 3beta-hydroxy-cholest-5-ene-25-hydroperoxide, a hydroperoxide identified in air-aged cholesterol. Thermal decomposition of 3beta-hydroxy-cholest-5-ene-25-hydroperoxide gives rise to 25-hydroxycholesterol
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
the enzyme contains a di-iron cofactor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
desmosterol
a potent inhibitor of CH25H
troleandomycin
specific inhibitor of CYP3A
desmosterol
a potent inhibitor of CH25H
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.77
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sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
patients with chronic obstructive pulmonary disease have increased expression of cholesterol 25-hydroxylase in the lung
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
transmembrane enzyme, prediction of transmembrane structures for CH25H subunits, overview
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
-
-
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31700
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x * 31700
31745
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x * 31745, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression in insect cell microsomes via baculovirus transfection
expression in COS cells, expression of cholesterol 25-hydroxylase in transfected cells reduces the biosynthesis of cholesterol from acetate and suppresses the cleavage of sterol regulatory element binding protein-1 and -2
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intronless gene CH25H is located on chromosome 10, DNA and amino acid sequence deterination and analysis, sequence comparisons, gene structures and tandem locations for the human CH25H and LIPA, EC 3.1.1.13, genes on chromosome 10
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recombinant expression in insect cell microsomes via baculovirus transfection
the gene encoding the enzyme is located on chromosome 10
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine