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Peroxisomes also play a role in the production of bile acids important for the absorption of fats and fat-soluble vitamins, such as vitamins A and K. Skin disorders are features of genetic disorders affecting peroxisome function as a result. [17] The specific metabolic pathways that occur exclusively in mammalian peroxisomes are: [5]
A peroxisome is a type of microbody that functions to help the body break down large molecules and detoxify hazardous substances. It contains enzymes like oxidase, react hydrogen peroxide as a byproduct of its enzymatic reactions. Within the peroxisome, hydrogen peroxide can then be converted to water by enzymes like catalase and peroxidase.
PPAR -alpha and -gamma pathways. In the field of molecular biology, the peroxisome proliferator–activated receptors (PPARs) are a group of nuclear receptor proteins that function as transcription factors regulating the expression of genes. [1]
224824 Ensembl ENSG00000124587 ENSMUSG00000002763 UniProt Q13608 Q99LC9 RefSeq (mRNA) NM_000287 NM_001316313 NM_145488 RefSeq (protein) NP_000278 NP_001303242 NP_663463 Location (UCSC) Chr 6: 42.96 – 42.98 Mb Chr 17: 47.02 – 47.04 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Peroxisome assembly factor 2 is a protein that in humans is encoded by the PEX6 gene. PEX6 is an AAA ...
Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) is a protein that in humans is encoded by the PPARGC1A gene. [4] PPARGC1A is also known as human accelerated region 20 . It may, therefore, have played a key role in differentiating humans from apes. [5] PGC-1α is the master regulator of mitochondrial biogenesis.
Peroxisome proliferator-activated receptor alpha (PPAR-α), also known as NR1C1 (nuclear receptor subfamily 1, group C, member 1), is a nuclear receptor protein functioning as a transcription factor that in humans is encoded by the PPARA gene. [5]
Peroxins serve several functions including the recognition of cytoplasmic proteins that contain peroxisomal targeting signals (PTS) that tag them for transport by peroxisomal proteins to the peroxisome.
Prxs were historically divided into three (mechanistic) classes: Typical 2-Cys Prxs; Atypical 2-Cys Prxs and; 1-Cys Prxs. The designation of "1-Cys" and "2-Cys" Prxs was introduced in 1994 [2] as it was noticed that, among the 22 Prx sequences known at the time, only one Cys residue was absolutely conserved; this is the residue now recognized as the (required) peroxidatic cysteine, C P.