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Basic structure of a peroxisome Distribution of peroxisomes (white) in HEK 293 cells during mitosis Peroxisome in rat neonatal cardiomyocyte. A peroxisome (/ p ə ˈ r ɒ k s ɪ ˌ s oʊ m /) [1] is a membrane-bound organelle, a type of microbody, found in the cytoplasm of virtually all eukaryotic cells. [2] [3] Peroxisomes are oxidative ...
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.
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.
The same enzymes are used in peroxisomes as in the mitochondrial matrix and acetyl-CoA is generated. Very long chain (greater than C-22) fatty acids, branched fatty acids, [9] some prostaglandins and leukotrienes [10] undergo initial oxidation in peroxisomes until octanoyl-CoA is formed, at which point it undergoes mitochondrial oxidation. [11]
Under the model of Kessler et al. (2008), the real functions of TPO are: [4] Conversion of iodide to diiodine , as in reaction (1) above. The I 2 produced would go on to react with OH − to form HOI , which reacts with the tyrosyl residue on proteins such as thyroglobulin, explaining the reactions (2) and (3) above.
The function of PPARs is modified by the precise shape of their ligand-binding domain (see below) induced by ligand binding and by a number of coactivator and corepressor proteins, the presence of which can stimulate or inhibit receptor function, respectively. [12] Endogenous ligands for the PPARs include free fatty acids, eicosanoids and ...
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.
All peroxisomal proteins are synthesized in the cytoplasm and must be directed to the peroxisome. [2] The first step in this process is the binding of the protein to a receptor. The receptor then directs the complex to the peroxisome. Receptors recognize and bind to a region of the peroxisomal protein called a peroxisomal targeting signal, or PTS.