| Gene Ontology | |
|---|---|
| Molecular function | • nucleotide binding • 3-hydroxyacyl-CoA dehydrogenase activity • receptor binding • long-chain-enoyl-CoA hydratase activity • isomerase activity • sterol binding • 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity • protein homodimerization activity • 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
| Cellular component | • peroxisome • peroxisomal membrane • peroxisomal matrix • intracellular membrane-bounded organelle |
| Biological process | • fatty acid beta-oxidation • bile acid biosynthetic process • bile acid metabolic process • androgen metabolic process • estrogen metabolic process • fatty acid beta-oxidation using acyl-CoA oxidase • unsaturated fatty acid metabolic process • alpha-linolenic acid metabolic process • very long-chain fatty-acyl-CoA metabolic process • medium-chain fatty-acyl-CoA metabolic process • cellular lipid metabolic process • small molecule metabolic process |
| Sources: Amigo / QuickGO | |
118.79 – 118.88 Mb
50.13 – 50.2 Mb
Peroxisomal multifunctional enzyme type 2 is a protein that in humans is encoded by the HSD17B4 gene.
The HSD17B4 gene encodes an enzyme involved in peroxisomal fatty acid beta-oxidation. It was first identified as a 17-beta-estradiol dehydrogenase (Leenders et al., 1996; van Grunsven et al., 1998). Peroxisomal beta-oxidation of fatty acids, originally described by Lazarow and de Duve (1976), is catalyzed by 3 enzymes: acyl-CoA oxidase (see, e.g., ACOX1, MIM 609751); the 'D-bifunctional enzyme,' with enoyl-CoA-hydratase and D-3-hydroxyacyl-CoA dehydrogenase activity, and 3-ketoacyl-CoA thiolase (MIM 604054).
See also the L-bifunctional peroxisomal protein (EHHADH; MIM 607037). The D- and L-bifunctional proteins have different substrate specificities. The D-bifunctional protein catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids and also acts in shortening cholesterol for bile acid formation. In contrast, the L-specific bifunctional protein does not have the latter 2 activities (Jiang et al., 1997).