HSD17B10 - hydroxysteroid 17-beta dehydrogenase 10 (human)
- Create:2016-09-14
- Modify:2025-01-29
The HSD17B10 gene provides instructions for making a protein called HSD10. This protein is located within mitochondria, the energy-producing centers inside cells, where it has several different functions.
The HSD10 protein is important for the production (synthesis) of proteins in mitochondria. (While most protein synthesis occurs in the fluid surrounding the nucleus, called the cytoplasm, a few proteins are synthesized in the mitochondria.) During protein synthesis, whether in the cytoplasm or in mitochondria, molecules called transfer RNAs (tRNAs) help assemble protein building blocks (amino acids) into the chains that form proteins. The HSD10 protein is involved in making functional mitochondrial tRNA. It forms a complex with an enzyme called TRMT10C to modify tRNAs so that they are more stable and can function properly. In addition, the complex interacts with another enzyme called PRORP to perform an enzymatic function called mitochondrial RNase P (mtRNase P) that cuts precursor RNA molecules, which is an essential step to generating tRNA molecules. Normal mitochondrial protein production, which requires tRNAs, is essential for the formation of the protein complexes that convert the energy from food into a form cells can use.
The HSD10 protein also plays an important role in processing several substances in the body. It helps break down the amino acid isoleucine. Specifically, it is responsible for the fifth step in this process, in which 2-methyl-3-hydroxybutyryl-CoA is converted into 2-methylacetoacetyl-CoA. Through a similar mechanism, the HSD10 protein also processes a group of fats called branched-chain fatty acids.
The HSD10 protein is also thought to be involved in chemical reactions involving female sex hormones (estrogens) and male sex hormones (androgens). HSD10 turns off (inactivates) a potent form of estrogen called 17β-estradiol by converting it to a weaker form called estrone. HSD10 also generates a potent androgen called dihydrotestosterone from a weak androgen called 3α-androstanediol. These reactions are critical for maintaining appropriate levels of male and female sex hormones.
The HSD10 protein also plays a role in certain chemical reactions involving neurosteroids, which are substances that regulate the activity of the nervous system. This protein inactivates two neurosteroids called allopregnanolone and allotetrahydrodeoxycorticosterone. These neurosteroids interact with receptors that prevent the brain from being overloaded with too many signals. By regulating the activity of these neurosteroids, the HSD10 protein may help maintain normal brain function. However, other proteins in the body can also carry out these reactions, and the importance of HSD10 in these functions is unclear.
- 17b-HSD10
- ABAD
- CAMR
- DUPXp11.22
- ERAB
- HADH2
- HCD2
- HSD10MD
- MHBD
- MRPP2
- MRX17
- MRX31
- MRXS10
- SCHAD
- SDR5C1
- 3-hydroxyacyl-CoA dehydrogenase type-2
- 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
- AB-binding alcohol dehydrogenase
- amyloid-beta peptide binding alcohol dehydrogenase
- endoplasmic reticulum-associated amyloid beta-peptide-binding protein
- mitochondrial RNase P subunit 2
- mitochondrial ribonuclease P protein 2
- short chain L-3-hydroxyacyl-CoA dehydrogenase type 2
- short chain type dehydrogenase/reductase XH98G2
- EC 1.1.1.159 7-alpha-hydroxysteroid dehydrogenase
- EC 1.1.1.178 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
- EC 1.1.1.239 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))
- EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase
- EC 1.1.1.53 3-alpha(or 20-beta)-hydroxysteroid dehydrogenase
- EC 1.1.1.62 17-beta-estradiol 17-dehydrogenase
Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PMID: 10600649, PMID: 12917011, PMID: 18996107, PMID: 19706438, PMID: 20077426, PMID: 25925575, PMID: 26950678, PMID: 28888424, PMID: 9553139). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PMID: 10600649, PMID: 12917011, PMID: 25925575, PMID: 26950678, PMID: 9553139). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PMID: 18996107, PMID: 19706438, PMID: 20077426). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PMID: 10600649, PMID: 12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PMID: 19706438, PMID: 28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PMID: 26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PMID: 9338779). Essential for structural and functional integrity of mitochondria (PMID: 20077426).
In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PMID: 18984158, PMID: 24549042, PMID: 25925575, PMID: 26950678, PMID: 28888424). Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PMID: 23042678, PMID: 29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PMID: 23042678, PMID: 25925575, PMID: 28888424). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PMID: 29040705). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
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