This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: acyl-CoA thioesterase pathway
|Superclasses:||Biosynthesis → Fatty Acid and Lipid Biosynthesis|
Fatty acids are often found in the cell in the activated form of an acyl-coA (see long-chain fatty acid activation). Acyl-CoAs are used in the biosynthesis of many cellular products and components. In plants they are involved in the biosynthesis of membrane lipids, seed storage lipids, wax, cutins and suberin.
Acyl-CoA thioesterase hydrolyzes fatty acyl-CoAs to free fatty acids. In eukaryotes, the enzyme activity has been detected in the cytosol, ER, mitochondrion and peroxisome. In prokaryotes, the enzymes activity is localized in the periplasm and cytosol. In prokaryotes acyl-CoA thiesterases are involved in catabolism, supporting growth on fatty acids or conjugated fatty acid as the sole source of carbon [Nie08a]. The physiological roles of acyl-CoA thioesterase in eukaryotic organisms remain unclear. Works in animal and yeast shed some preliminary clue about the involvement of the enzyme in fatty acid oxidation. ACH2 is the first cloned plant acyl-CoA thioesterase [Tilton04]. The gene is highly expressed in mature tissues rather than in germinating seedlings where fatty acid beta-oxidation predominantly occurs. It indicates the role of ACH2 is not linked to fatty acid oxidation.
Unification Links: AraCyc:PWY-5148
Molina09: Molina I, Li-Beisson Y, Beisson F, Ohlrogge JB, Pollard M (2009). "Identification of an Arabidopsis feruloyl-coenzyme A transferase required for suberin synthesis." Plant Physiol 151(3);1317-28. PMID: 19759341
Nie08a: Nie L, Ren Y, Janakiraman A, Smith S, Schulz H (2008). "A novel paradigm of fatty acid beta-oxidation exemplified by the thioesterase-dependent partial degradation of conjugated linoleic acid that fully supports growth of Escherichia coli." Biochemistry 47(36);9618-26. PMID: 18702504
Barnes68: Barnes EM, Wakil SJ (1968). "Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase." J Biol Chem 1968;243(11);2955-62. PMID: 4871199
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Ichihara93: Ichihara S, Matsubara Y, Kato C, Akasaka K, Mizushima S (1993). "Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants." J Bacteriol 175(4);1032-7. PMID: 8432696
Jiang94: Jiang P, Cronan JE (1994). "Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action." J Bacteriol 176(10);2814-21. PMID: 7910602
Karasawa91: Karasawa K, Kudo I, Kobayashi T, Homma H, Chiba N, Mizushima H, Inoue K, Nojima S (1991). "Lysophospholipase L1 from Escherichia coli K-12 overproducer." J Biochem (Tokyo) 109(2);288-93. PMID: 1864840
Karasawa99: Karasawa K, Yokoyama K, Setaka M, Nojima S (1999). "The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively." J Biochem (Tokyo) 1999;126(2);445-8. PMID: 10423542
Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744
Lee06: Lee LC, Lee YL, Leu RJ, Shaw JF (2006). "Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1." Biochem J 397(1);69-76. PMID: 16515533
Lee07d: Lee LC, Liaw YC, Lee YL, Shaw JF (2007). "Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L(1)." Biochim Biophys Acta 1774(8);959-67. PMID: 17604237
Lee09b: Lee LC, Chou YL, Chen HH, Lee YL, Shaw JF (2009). "Functional role of a non-active site residue Trp(23) on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L(1)." Biochim Biophys Acta 1794(10);1467-73. PMID: 19540368
Lee97b: Lee YL, Chen JC, Shaw JF (1997). "The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates." Biochem Biophys Res Commun 231(2);452-6. PMID: 9070299
Li00a: Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS (2000). "Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme." Nat Struct Biol 7(7);555-9. PMID: 10876240
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