チオエステラーゼ
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/05/03 03:10:41」(JST)
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Thioesterases are enzymes which belong to the Esterase family. Esterases, in turn, are one type of the several hydrolases known.
Thioesterases exhibit Esterase activity (splitting of an ester into acid and alcohol, in the presence of water) specifically at a thiol group.
Thioesterases or thiolester hydrolases are identified as members of E.C.3.1.2.
Examples
Acetyl-coA hydrolase, palmitoyl-coA hydrolase, succinyl-coA hydrolase, formyl-coA hydrolase, acyl-coA hydrolase are a few examples of this group of enzymes.
Ubiquitin thiolesterase is a well-known example, whose structure has been analyzed.
Humans genes which encode thiolesterases include:[1]
ACOT1, ACOT2, ACOT4, ACOT6, ACOT7, ACOT8, ACOT9, ACOT11(STARD14), ACOT12 (STARD15), OLAH, PPT1, PPT2, THEM2 (ACOT13), THEM4, THEM4P1, THEM5
References
- ^ Brocker, C; Carpenter, C; Nebert, DW; Vasiliou, V (Aug 2010). "Evolutionary divergence and functions of the human acyl-CoA thioesterase gene ( ACOT ) family.". Human Genomics 4 (6): 411–20. PMC 3525216. PMID 20846931.
External links
- thioesterase I at the US National Library of Medicine Medical Subject Headings (MeSH)
- thioesterase II at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: esterases (EC 3.1)
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3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
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3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
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3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
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Exoribonuclease |
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3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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English Journal
- Synthesis of medium chain length fatty acid ethyl esters in engineered Escherichia coli using endogenously produced medium chain fatty acids.
- Fan L, Liu J, Nie K, Liu L, Wang F, Tan T, Deng L.SourceBeijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China.
- Enzyme and microbial technology.Enzyme Microb Technol.2013 Jul 10;53(2):128-33. doi: 10.1016/j.enzmictec.2013.03.012. Epub 2013 Mar 31.
- Microbial biosynthesis of fatty acid-derived biofuels from renewable carbon sources has attracted significant attention in recent years. Free fatty acids (FFAs) can be used as precursors for the production of micro-diesel. The expression of codon optimized two plants (Umbellularia californica and Ci
- PMID 23769314
- LovG: The Thioesterase Required for Dihydromonacolin L Release and Lovastatin Nonaketide Synthase Turnover in Lovastatin Biosynthesis.
- Xu W, Chooi YH, Choi JW, Li S, Vederas JC, Da Silva NA, Tang Y.SourceDepartment of Chemical and Biomolecular Engineering, Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095 (USA).
- Angewandte Chemie (International ed. in English).Angew Chem Int Ed Engl.2013 Jun 17;52(25):6472-5. doi: 10.1002/anie.201302406. Epub 2013 May 7.
- No Lov lost: The cryptic thioesterase LovG was found to be responsible for product release from the lovastatin nonaketide synthase (LNKS or LovB; see scheme). LovG also helped improve the turnover of LovB through hydrolysis of incorrectly made intermediates, freeing LovB for another round of catalys
- PMID 23653178
- Pathogenesis and therapies for infantile neuronal ceroid lipofuscinosis (infantile CLN1 disease).
- Hawkins-Salsbury JA, Cooper JD, Sands MS.SourceWashington University School of Medicine, Department of Internal Medicine, Box 8007, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
- Biochimica et biophysica acta.Biochim Biophys Acta.2013 Jun 6. pii: S0925-4439(13)00188-9. doi: 10.1016/j.bbadis.2013.05.026. [Epub ahead of print]
- The neuronal ceroid lipofuscinoses (NCL, Batten disease) are a group of inherited neurodegenerative diseases. Infantile neuronal ceroid lipofuscinosis (INCL, infantile Batten disease, or infantile CLN1 disease) is caused by a deficiency in the soluble lysosomal enzyme palmitoyl protein thioesterase-
- PMID 23747979
Japanese Journal
- Upregulation of Fatty Acyl-CoA Thioesterases in the Heart and Skeletal Muscle of Rats Fed a High-Fat Diet
- Fujita Mariko,Momose Atsushi,Ohtomo Takayuki,Nishinosono Azusa,Tanonaka Kouichi,Toyoda Hiroo,Morikawa Masako,Yamada Junji
- Biological & Pharmaceutical Bulletin 34(1), 87-91, 2011
- … We examined the hypothesis that, because of its catalytic properties, acyl-CoA thioesterase (ACOT) would counteract these detrimental situations by modulating intracellular acyl-CoA levels. …
- NAID 130000402268
- Genetic replacement of tesB with PTE1 affects chain-length proportions of 3-hydroxyalkanoic acids produced through β-oxidation of oleic acid in Escherichia coli(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Seto Yoshiaki,Kang Junkyu,Li Ming,Habu Naoto,Nihei Ken-ichi,Ueda Shunsaku,Maeda Isamu
- Journal of bioscience and bioengineering 110(4), 392-396, 2010-10
- … Acyl-CoA thioesterase II (TesB), which catalyzes hydrolysis of acyl-CoAs to free fatty acids and CoA, is involved in 3-hydroxyalkanoic acid production in Escherichia coli. … Effects of genetic replacement of tesB with Saccharomyces cerevisiae acyl-CoA thioesterase gene PTE1 on 3-hydroxyalkanoic acid production from oleic acid through β-oxidation were examined. …
- NAID 110007880134
Related Links
- Thioesterases are enzymes which belong to the Esterase family. Esterases, in turn, are one type of the several hydrolases known. Thioesterases exhibit Esterase activity (splitting of an ester into acid and alcohol, in the presence of water) ...
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