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| ACOT8 | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Competes with bile acid CoA-amino acid N-acyltransferase (BAAT) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (C2 to C20). Inactive towards substrates with more than C20 aliphatic chains. Involved in the metabolic regulation of peroxisome p [...] (319 aa) | |||
| DECR2 | Peroxisomal 2,4-dienoyl-CoA reductase; Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid; Belongs to the short-chain dehydrogenases/reducta [...] (292 aa) | |||
| DAO | D-amino-acid oxidase; Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids; Belongs to the DAMOX/DASOX family (347 aa) | |||
| RBP2 | Retinol-binding protein 2; Intracellular transport of retinol; Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family (134 aa) | |||
| RBP1 | Retinol-binding protein 1; Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis; Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family (197 aa) | |||
| ACOT2 | Acyl-coenzyme A thioesterase 2, mitochondrial; Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs (483 aa) | |||
| BCO1 | Beta,beta-carotene 15,15’-dioxygenase; Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism; Belongs to the carotenoid oxygenase family (547 aa) | |||
| BAAT | Bile acid-CoA-amino acid N-acyltransferase; Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile aci [...] (418 aa) | |||
| PECR | Peroxisomal trans-2-enoyl-CoA reductase; Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity; Short chain dehydrogenase/reductase superfamily (303 aa) | |||
| IDE | Insulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases (1019 aa) | |||
| RBP5 | Retinol-binding protein 5; Intracellular transport of retinol; Fatty acid binding protein family (135 aa) | |||
| NUDT7 | Peroxisomal coenzyme A diphosphatase NUDT7; Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3’,5’-ADP and the corresponding 4’-phosphopantetheine derivative as products. CoA into 3’,5’-ADP and 4’- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5’-triphosphates, nucleoside 5’-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5’-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA [...] (238 aa) | |||
| PAOX | Peroxisomal N(1)-acetyl-spermine/spermidine oxidase; Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity- N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs; Belongs to the flavin m [...] (511 aa) | |||
| LONP2 | Lon protease homolog 2, peroxisomal; ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1; AAA ATPases (852 aa) | |||
| TYSND1 | Peroxisomal leader peptide-processing protease; Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta- oxidation of fatty acids (566 aa) | |||
| PEX10 | Peroxisome biogenesis factor 10; Somewhat implicated in the biogenesis of peroxisomes; Peroxins (346 aa) | |||
| PEX13 | Peroxisomal membrane protein PEX13; Component of the peroxisomal translocation machinery with PEX14 and PEX17. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1 and PTS2 proteins; Peroxins (403 aa) | |||
| RETSAT | All-trans-retinol 13,14-reductase; Catalyzes the saturation of all-trans-retinol to all- trans-13,14-dihydroretinol. Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers. May play a role in the metabolism of vitamin A. Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP. May play a role in adipocyte differentiation; Belongs to the carotenoid/retinoid oxidoreductase family. CrtISO subfamily (610 aa) | |||
| AGXT | Alanine-glyoxylate aminotransferase (392 aa) | |||
| CRAT | Carnitine O-acetyltransferase; Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria; Belongs to the carnitine/choline acetyltransferase family (626 aa) | |||
| PIPOX | Peroxisomal sarcosine oxidase; Metabolizes sarcosine, L-pipecolic acid and L-proline (390 aa) | |||
| ACOT4 | Acyl-coenzyme A thioesterase 4; Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (By similarity). Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs; Belongs to the C/M/P thioester hydrolase family (421 aa) | |||
| HACL1 | 2-hydroxyacyl-CoA lyase 1; Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde; Belongs to the TPP enzyme family (578 aa) | |||
| DHRS4 | Dehydrogenase/reductase SDR family member 4; Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co- factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones (By similarity); Belongs to the short-chain dehydrogenases/reductases (SDR) family (278 aa) | |||
| NOS2 | Nitric oxide synthase, inducible; Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on ’Cys-247’ implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR [...] (1153 aa) | |||
| LRAT | Lecithin retinol acyltransferase; Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments; [...] (230 aa) | |||
