Cholesterol 25-hydroxylase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.99.38 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a cholesterol 25-hydroxylase (EC 1.14.99.38) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are cholesterol, an electron acceptor AH2, and O2, whereas its 3 products are 25-hydroxycholesterol (25HC), the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is cholesterol, hydrogen-donor:oxygen oxidoreductase (25-hydroxylating). This enzyme is also called cholesterol 25-monooxygenase.
Transcripts for this enzyme have been identified in macrophages from the testis.
CH25H is an interferon-stimulated gene, and its primary product 25HC may have broad-spectrum antiviral activity, demonstrated in mice against HIV, ebola, Nipah virus, Rift Valley Fever virus, and SARS-CoV-2. Specifically, 25HC blocks membrane fusion between the cell and virus, and may "implicate membrane-modifying oxysterols as potential antiviral therapeutics.” Recently, upregulation of CH25H has been shown to play a role in effectively restricting infection of lung epithelial cells with SARS-Cov-2 through its enzymatic product, 25HC, which depletes accessible membrane cholesterol so that the virus is unable to achieve fusion with the cell membrane necessary for entry and infection. [1]
It has been proposed, based on experimental research in both mice and human cell culture, that 25HC is a potent senolytic. Further research needs to elaborate on this research and reveal its true significance to aging. [2]
In enzymology, a 24-hydroxycholesterol 7alpha-hydroxylase (EC 1.14.13.99) is an enzyme that catalyzes the chemical reaction
In enzymology, a 27-hydroxycholesterol 7alpha-monooxygenase (EC 1.14.13.60) is an enzyme that catalyzes the chemical reaction
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7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase (EC 1.14.14.139, previously EC 1.14.13.95) is an enzyme that catalyzes the chemical reaction:
Cholesterol 24-hydroxylase, also commonly known as cholesterol 24S-hydroxylase, cholesterol 24-monooxygenase, CYP46, or CYP46A1, is an enzyme that catalyzes the conversion of cholesterol to 24S-hydroxycholesterol. It is responsible for the majority of cholesterol turnover in the human central nervous system. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating).
In enzymology, a cholesterol 7alpha-monooxygenase (EC 1.14.13.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a deoxyhypusine monooxygenase (EC 1.14.99.29) is an enzyme that catalyzes the chemical reaction
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In enzymology, an isoflavone 3'-hydroxylase (EC 1.14.14.88, Formerly EC 1.14.13.52) is an enzyme that catalyzes the chemical reaction
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G-protein coupled receptor 183 also known as Epstein-Barr virus-induced G-protein coupled receptor 2 (EBI2) is a protein (GPCR) expressed on the surface of some immune cells, namely B cells and T cells; in humans it is encoded by the GPR183 gene. Expression of EBI2 is one critical mediator of immune cell localization within lymph nodes, responsible in part for the coordination of B cell, T cell, and dendritic cell movement and interaction following antigen exposure. EBI2 is a receptor for oxysterols. The most potent activator is 7α,25-dihydroxycholesterol (7α,25-OHC), with other oxysterols exhibiting varying affinities for the receptor. Oxysterol gradients drive chemotaxis, attracting the EBI2-expressing cells to locations of high ligand concentration. The GPR183 gene was identified due to its upregulation during Epstein-Barr virus infection of the Burkitt's lymphoma cell line BL41, hence its name: EBI2.
25-hydroxycholesterol 7-alpha-hydroxylase also known as oxysterol and steroid 7-alpha-hydroxylase is an enzyme that in humans is encoded by the CYP7B1 gene. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids.
25-hydroxycholesterol 7alpha-hydroxylase (EC 1.14.13.100, 25-hydroxycholesterol 7alpha-monooxygenase, CYP7B1, CYP7B1 oxysterol 7alpha-hydroxylase) is an enzyme with systematic name cholest-5-ene-3beta,25-diol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). This enzyme catalyses the following chemical reaction
24S-Hydroxycholesterol (24S-HC), also known as cholest-5-ene-3,24-diol or cerebrosterol, is an endogenous oxysterol produced by neurons in the brain to maintain cholesterol homeostasis. It was discovered in 1953 by Alberto Ercoli, S. Di Frisco, and Pietro de Ruggieri, who first isolated the molecule in the horse brain and then demonstrated its presence in the human brain.
25-Hydroxycholesterol is a chemical compound, a derivative of cholesterol, that plays a role in various biological processes in humans and other species. It is involved in cholesterol metabolism, antivirus process, inflammatory and immune response, and survival signaling pathway. 25-hydroxycholesterol is biosynthesized from cholesterol by adding a hydroxyl group at position 25-carbon of a steroid nucleus. This reaction is catalyzed by cholesterol 25-hydroxylase, a family of enzymes that use oxygen and a di-iron cofactor to catalyze hydroxylation reaction.