ACOT8: Difference between revisions

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Latest revision as of 17:44, 29 August 2017

Acyl-coenzyme A thioesterase 8 is an enzyme that in humans is encoded by the ACOT8 gene.^[1]^[2]^[3]^[4]^[5]

The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. Multiple transcript variants encoding several different isoforms have been found for this gene.^[5]

References

↑ Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ (Apr 1999). "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans". J Biol Chem. 274 (14): 9216–23. doi:10.1074/jbc.274.14.9216. PMID 10092594.
↑ Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S (Jul 1997). "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation". J Biol Chem. 272 (21): 13779–85. doi:10.1074/jbc.272.21.13779. PMID 9153233.
↑ Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE (Aug 2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029–32. doi:10.1194/jlr.E500003-JLR200. PMID 16103133.
↑ Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE (Aug 2006). "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs". FASEB J. 20 (11): 1855–64. doi:10.1096/fj.06-6042com. PMID 16940157.
↑ ^5.0 ^5.1 "Entrez Gene: ACOT8 acyl-CoA thioesterase 8".

Hunt MC, Alexson SE (2002). "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism". Prog. Lipid Res. 41 (2): 99–130. doi:10.1016/S0163-7827(01)00017-0. PMID 11755680.
Watanabe H, Shiratori T, Shoji H, et al. (1997). "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef". Biochem. Biophys. Res. Commun. 238 (1): 234–9. doi:10.1006/bbrc.1997.7217. PMID 9299485.
Liu LX, Heveker N, Fackler OT, et al. (2000). "Mutation of a Conserved Residue (D123) Required for Oligomerization of Human Immunodeficiency Virus Type 1 Nef Protein Abolishes Interaction with Human Thioesterase and Results in Impairment of Nef Biological Functions". J. Virol. 74 (11): 5310–9. doi:10.1128/JVI.74.11.5310-5319.2000. PMC 110886. PMID 10799608.
Cohen GB, Rangan VS, Chen BK, et al. (2000). "The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation". J. Biol. Chem. 275 (30): 23097–105. doi:10.1074/jbc.M000536200. PMID 10807905.
Jones JM, Gould SJ (2000). "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase". Biochem. Biophys. Res. Commun. 275 (1): 233–40. doi:10.1006/bbrc.2000.3285. PMID 10944470.
Fossey SC, Mychaleckyj JC, Pendleton JK, et al. (2001). "A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20". Genomics. 76 (1–3): 45–57. doi:10.1006/geno.2001.6584. PMID 11549316.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Ishizuka M, Toyama Y, Watanabe H, et al. (2004). "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis". Exp. Cell Res. 297 (1): 127–41. doi:10.1016/j.yexcr.2004.02.029. PMID 15194431.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Westin MA, Hunt MC, Alexson SE (2006). "The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes". J. Biol. Chem. 280 (46): 38125–32. doi:10.1074/jbc.M508479200. PMID 16141203.
Takagi M, Suto F, Suga T, Yamada J (2006). "Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription". Mol. Cell. Biochem. 275 (1–2): 199–206. doi:10.1007/s11010-005-1990-y. PMID 16335799.
Yamaori S, Ukena E, Fujiyama N, et al. (2007). "Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase". Xenobiotica. 37 (3): 260–70. doi:10.1080/00498250601167091. PMID 17624024.

External links

ACOT8 human gene location in the UCSC Genome Browser.
ACOT8 human gene details in the UCSC Genome Browser.

This article on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

[pmid10092594-1] Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ (Apr 1999). "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans". J Biol Chem. 274 (14): 9216–23. doi:10.1074/jbc.274.14.9216. PMID 10092594.

[pmid9153233-2] Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S (Jul 1997). "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation". J Biol Chem. 272 (21): 13779–85. doi:10.1074/jbc.272.21.13779. PMID 9153233.

[pmid16103133-3] Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE (Aug 2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029–32. doi:10.1194/jlr.E500003-JLR200. PMID 16103133.

[pmid16940157-4] Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE (Aug 2006). "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs". FASEB J. 20 (11): 1855–64. doi:10.1096/fj.06-6042com. PMID 16940157.

[entrez-5] 5.0 ^5.1 "Entrez Gene: ACOT8 acyl-CoA thioesterase 8".

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Acyl-coenzyme A thioesterase 8''' is an [[enzyme]] that in [[human]]s is encoded by the ''ACOT8'' [[gene]].<ref name="pmid10092594">{{cite journal | vauthors = Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ | title = Identification of peroxisomal acyl-CoA thioesterases in yeast and humans | journal = J Biol Chem | volume = 274 | issue = 14 | pages = 9216–23 |date=Apr 1999 | pmid = 10092594 | pmc =  | doi =10.1074/jbc.274.14.9216  }}</ref><ref name="pmid9153233">{{cite journal | vauthors = Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S | title = Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation | journal = J Biol Chem | volume = 272 | issue = 21 | pages = 13779–85 |date=Jul 1997 | pmid = 9153233 | pmc =  | doi =10.1074/jbc.272.21.13779  }}</ref><ref name="pmid16103133">{{cite journal | vauthors = Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE | title = A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases | journal = J Lipid Res | volume = 46 | issue = 9 | pages = 2029–32 |date=Aug 2005 | pmid = 16103133 | pmc =  | doi = 10.1194/jlr.E500003-JLR200 }}</ref><ref name="pmid16940157">{{cite journal | vauthors = Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE | title = Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs | journal = FASEB J | volume = 20 | issue = 11 | pages = 1855–64 |date=Aug 2006 | pmid = 16940157 | pmc =  | doi = 10.1096/fj.06-6042com }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACOT8 acyl-CoA thioesterase 8| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005| accessdate = }}</ref>
-| update_page = yes
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-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Acyl-CoA thioesterase 8
- | HGNCid = 15919
- | Symbol = ACOT8
- | AltSymbols =; HNAACTE; PTE1; PTE2; hACTE-III; hTE
- | OMIM = 608123
- | ECnumber =
- | Homologene = 3991
- | MGIid = 2158201
-  | GeneAtlas_image1 = PBB_GE_ACOT8_204212_at_tn.png
-  | Function = {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008778 |text = acyl-CoA thioesterase II activity}} {{GNF_GO|id=GO:0016290 |text = palmitoyl-CoA hydrolase activity}} {{GNF_GO|id=GO:0016291 |text = acyl-CoA thioesterase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
- | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
-  | Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006637 |text = acyl-CoA metabolic process}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 10005
-    | Hs_Ensembl = ENSG00000101473
-    | Hs_RefseqProtein = NP_899241
-    | Hs_RefseqmRNA = NM_183385
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 20
-    | Hs_GenLoc_start = 43903768
-    | Hs_GenLoc_end = 43919442
-    | Hs_Uniprot = O14734
-    | Mm_EntrezGene = 170789
-    | Mm_Ensembl = ENSMUSG00000017307
-    | Mm_RefseqmRNA = NM_133240
-    | Mm_RefseqProtein = NP_573503
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 164483705
-    | Mm_GenLoc_end = 164496413
-    | Mm_Uniprot = Q3U965
-  }}
-}}
-'''Acyl-CoA thioesterase 8''', also known as '''ACOT8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACOT8 acyl-CoA thioesterase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. Multiple transcript variants encoding several different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ACOT8 acyl-CoA thioesterase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005| accessdate = }}</ref>
+| summary_text = The protein encoded by this gene is a [[peroxisomal]] [[thioesterase]] that appears to be involved more in the [[oxidation]] of [[fatty acid]]s rather than in their formation. The encoded protein can bind to the human [[immunodeficiency]] [[virus]]-1 protein [[Nef (protein)|Nef]], and mediate Nef-induced down-regulation of [[CD4]] in [[T-cells]]. Multiple transcript variants encoding several different [[isoform]]s have been found for this gene.<ref name="entrez"/>
 }}
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Hunt MC, Alexson SE |title=The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. |journal=Prog. Lipid Res. |volume=41 |issue= 2 |pages= 99-130 |year= 2002 |pmid= 11755680 |doi=  }}
+*{{cite journal  | vauthors=Hunt MC, Alexson SE |title=The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism |journal=Prog. Lipid Res. |volume=41 |issue= 2 |pages= 99–130 |year= 2002 |pmid= 11755680 |doi=10.1016/S0163-7827(01)00017-0  }}
-*{{cite journal  | author=Liu LX, Margottin F, Le Gall S, ''et al.'' |title=Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13779-85 |year= 1997 |pmid= 9153233 |doi=  }}
+*{{cite journal  | vauthors=Watanabe H, Shiratori T, Shoji H |title=A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 1 |pages= 234–9 |year= 1997 |pmid= 9299485 |doi= 10.1006/bbrc.1997.7217 |display-authors=etal}}
-*{{cite journal  | author=Watanabe H, Shiratori T, Shoji H, ''et al.'' |title=A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 1 |pages= 234-9 |year= 1997 |pmid= 9299485 |doi= 10.1006/bbrc.1997.7217 }}
+*{{cite journal  | vauthors=Liu LX, Heveker N, Fackler OT |title=Mutation of a Conserved Residue (D123) Required for Oligomerization of Human Immunodeficiency Virus Type 1 Nef Protein Abolishes Interaction with Human Thioesterase and Results in Impairment of Nef Biological Functions |journal=J. Virol. |volume=74 |issue= 11 |pages= 5310–9 |year= 2000 |pmid= 10799608 |doi=10.1128/JVI.74.11.5310-5319.2000  | pmc=110886  |display-authors=etal}}
-*{{cite journal  | author=Jones JM, Nau K, Geraghty MT, ''et al.'' |title=Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9216-23 |year= 1999 |pmid= 10092594 |doi=  }}
+*{{cite journal  | vauthors=Cohen GB, Rangan VS, Chen BK |title=The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23097–105 |year= 2000 |pmid= 10807905 |doi= 10.1074/jbc.M000536200 |display-authors=etal}}
-*{{cite journal  | author=Liu LX, Heveker N, Fackler OT, ''et al.'' |title=Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions. |journal=J. Virol. |volume=74 |issue= 11 |pages= 5310-9 |year= 2000 |pmid= 10799608 |doi=  }}
+*{{cite journal  | vauthors=Jones JM, Gould SJ |title=Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 233–40 |year= 2000 |pmid= 10944470 |doi= 10.1006/bbrc.2000.3285 }}
-*{{cite journal  | author=Cohen GB, Rangan VS, Chen BK, ''et al.'' |title=The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23097-105 |year= 2000 |pmid= 10807905 |doi= 10.1074/jbc.M000536200 }}
+*{{cite journal  | vauthors=Fossey SC, Mychaleckyj JC, Pendleton JK |title=A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20 |journal=Genomics |volume=76 |issue= 1–3 |pages= 45–57 |year= 2001 |pmid= 11549316 |doi= 10.1006/geno.2001.6584 |display-authors=etal}}
-*{{cite journal  | author=Jones JM, Gould SJ |title=Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 233-40 |year= 2000 |pmid= 10944470 |doi= 10.1006/bbrc.2000.3285 }}
+*{{cite journal  | vauthors=Deloukas P, Matthews LH, Ashurst J |title=The DNA sequence and comparative analysis of human chromosome 20 |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a |display-authors=etal}}
-*{{cite journal  | author=Fossey SC, Mychaleckyj JC, Pendleton JK, ''et al.'' |title=A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20. |journal=Genomics |volume=76 |issue= 1-3 |pages= 45-57 |year= 2001 |pmid= 11549316 |doi= 10.1006/geno.2001.6584 }}
+*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
-*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
+*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal  | vauthors=Ishizuka M, Toyama Y, Watanabe H |title=Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis |journal=Exp. Cell Res. |volume=297 |issue= 1 |pages= 127–41 |year= 2004 |pmid= 15194431 |doi= 10.1016/j.yexcr.2004.02.029 |display-authors=etal}}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
-*{{cite journal  | author=Ishizuka M, Toyama Y, Watanabe H, ''et al.'' |title=Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. |journal=Exp. Cell Res. |volume=297 |issue= 1 |pages= 127-41 |year= 2004 |pmid= 15194431 |doi= 10.1016/j.yexcr.2004.02.029 }}
+*{{cite journal  | vauthors=Westin MA, Hunt MC, Alexson SE |title=The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38125–32 |year= 2006 |pmid= 16141203 |doi= 10.1074/jbc.M508479200 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  | vauthors=Takagi M, Suto F, Suga T, Yamada J |title=Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription |journal=Mol. Cell. Biochem. |volume=275 |issue= 1–2 |pages= 199–206 |year= 2006 |pmid= 16335799 |doi=10.1007/s11010-005-1990-y  }}
-*{{cite journal  | author=Hunt MC, Yamada J, Maltais LJ, ''et al.'' |title=A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. |journal=J. Lipid Res. |volume=46 |issue= 9 |pages= 2029-32 |year= 2005 |pmid= 16103133 |doi= 10.1194/jlr.E500003-JLR200 }}
+*{{cite journal  | vauthors=Yamaori S, Ukena E, Fujiyama N |title=Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase |journal=Xenobiotica |volume=37 |issue= 3 |pages= 260–70 |year= 2007 |pmid= 17624024 |doi=10.1080/00498250601167091  |display-authors=etal}}
-*{{cite journal  | author=Westin MA, Hunt MC, Alexson SE |title=The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38125-32 |year= 2006 |pmid= 16141203 |doi= 10.1074/jbc.M508479200 }}
-*{{cite journal  | author=Takagi M, Suto F, Suga T, Yamada J |title=Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription. |journal=Mol. Cell. Biochem. |volume=275 |issue= 1-2 |pages= 199-206 |year= 2006 |pmid= 16335799 |doi=  }}
-*{{cite journal  | author=Hunt MC, Rautanen A, Westin MA, ''et al.'' |title=Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. |journal=FASEB J. |volume=20 |issue= 11 |pages= 1855-64 |year= 2006 |pmid= 16940157 |doi= 10.1096/fj.06-6042com }}
-*{{cite journal  | author=Yamaori S, Ukena E, Fujiyama N, ''et al.'' |title=Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase. |journal=Xenobiotica |volume=37 |issue= 3 |pages= 260-70 |year= 2007 |pmid= 17624024 |doi=  }}
 }}
 {{refend}}
-{{protein-stub}}
+==External links==
-{{WikiDoc Sources}}
+* {{UCSC genome browser|ACOT8}}
+* {{UCSC gene details|ACOT8}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
+{{Thioesterases}}
+[[Category:Human proteins]]
+{{gene-20-stub}}

v t e Thioesterases (EC 3.1.2)
Acetyl-CoA thioesterases
Acyl-CoA thioesterases	ACOT1 ACOT2 ACOT4 ACOT6 ACOT7 ACOT8 ACOT9 ACOT11 ACOT12 ACOT13
Formyl-CoA thioesterases
Palmitoyl protein thioesterases	PPT1 PPT2
Succinyl-CoA thioesterases
Ubiquitin C-terminal hydrolases	UCHL1 UCHL3 UCHL5

ACOT8: Difference between revisions

Latest revision as of 17:44, 29 August 2017

References

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