Regular ArticleShort-Chain 3-Hydroxy-2-methylacyl-CoA Dehydrogenase from Rat Liver: Purification and Characterization of a Novel Enzyme of Isoleucine Metabolism
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Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes
2024, Journal of Biological ChemistryStructural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes
2022, Trends in Biochemical SciencesCitation Excerpt :In contrast to the widespread ssPRORPs, msPRORPs have thus far only been found in mitochondria of metazoans [21,50]. In humans, the mtRNase P is a trimeric complex comprised of an endonuclease, a methyltransferase, and a fatty acid/sterol dehydrogenase [21,51,52]. Its nucleolytic subunit Homo sapiens PRORP (hsPRORP; also known as MRPP3) is an orthologue of ssPRORPs and exhibits a high degree of sequence similarity to the ssPRORPs from A. thaliana and T. brucei [23,53].
17B-hydroxysteroid dehydrogenases as acyl thioester metabolizing enzymes
2019, Molecular and Cellular EndocrinologyCitation Excerpt :It may seem prudent to therefore refer to HSD17B10 as a multitasking rather than multifunctional protein to distinguish between these arrangements. The protein was initially purified from rat liver as 3-hydroxy-2-methylacyl-CoA dehydrogenase of isoleucine metabolism (Luo et al., 1995) and cloned as short-chain 3S-hydroxyacyl-CoA dehydrogenase (SCHAD) involved in β-oxidation by screening of a human liver cDNA library (Vredendaal et al., 1996) for the homolog of an enzyme that had been previously isolated from pig heart (Noyes and Bradshaw, 1973). The same protein was also cloned by screening a bovine liver cDNA expression library using antibody raised against the purified 3-hydroxyacyl-CoA dehydrogenase type II (HADH2) (Furuta et al., 1997).
17β-Hydroxysteroid dehydrogenases and neurosteroid metabolism in the central nervous system
2019, Molecular and Cellular EndocrinologyCitation Excerpt :Each subunit has 261 amino acid residues with an isoelectric pH 7.65. Its rat homolog was first isolated from rat liver and characterized as a 2-methyl-3-hydroxyacyl dehydrogenase essential for the catalysis of the isoleucine degradation pathway (Luo et al., 1995). Thereafter, a bovine homolog was isolated from bovine liver as type II 3-hydroxyacyl-CoA dehydrogenase (Kobayashi et al., 1996).
Serum metabolomics study in a group of Parkinson's disease patients from northern India
2018, Clinica Chimica ActaCitation Excerpt :2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) is a mitochondrial enzyme involved in the catabolism of isoleucine and branched-chain fatty acids. MHBD deficiency causes impaired catabolism of isoleucine presenting as neurodegenerative disease [7]. Glutamate metabolism changes take place in many neurodegenerative pathologies, and the disruptions may be related to changes of glutamate metabolism enzyme activities, alterations of the main energy formation reactions in mitochondria, and shifts of oxidation/redox balance in cells.
Novel patient missense mutations in the HSD17B10 gene affect dehydrogenase and mitochondrial tRNA modification functions of the encoded protein
2017, Biochimica et Biophysica Acta - Molecular Basis of DiseaseCitation Excerpt :HSD10/MRPP2 belongs to the family of NAD(P)(H)-dependent short-chain dehydrogenase/reductases (SDR) [1–3], and was first identified as the dehydrogenase enzyme L-2-methyl-3-hydroxyacyl-CoA dehydrogenase (L-methyl-3-HAD) that converts L-2-methyl-3-hydroxybutyryl-CoA to 2-methyl-acetoacetyl-CoA, the penultimate step of isoleucine metabolism by β-oxidation [4]. Since then, many in vitro SDR substrates have been identified for HSD10/MRPP2 including the sex hormone 17β-estradiol [5,6], bile acids [7], the neurosteroid allopregnanolone [8], and short straight-chain/branched-chain fatty acyl-CoA thioesters [9]. The protein is also known to be inhibited by amyloid-β peptide [10,11].