Thioesterase: Difference between revisions

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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-{{STRUCTURE_1u8u|  PDB=1u8u  | SIZE=400| SCENE= |right|CAPTION=E. Coli Acyl-CoA thioesterase complex with octanoic acid, [[1u8u]] }}
+<StructureSection load='' size='350' side='right' caption='Human ubiquitin esterase 2 (deepskyblue) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code [[2hd5]]).' scene='48/489265/Cv/2'>
+__TOC__
+== Function ==
+'''Thioesterase''' (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group.  TEs are substrate-specific.<br />
+*  '''Palmitoyl protein TE''' removes fatty acids like palmitate from modified cysteine residues during lysosomal degradation<ref>PMID:10737604</ref>.  For details see [[Palmitoyl protein thioesterase]].<br />
+*  '''4-hydroxybenzoyl-CoA TE''' converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA<ref>PMID:12732540</ref>.<br />
+*  '''Acyl-CoA TE''' hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism<ref>PMID:11755680</ref>.  See also [[YbgC]] and [[Mitochondrial hotdog-fold thioesterase]].<br />
+*   '''Fluoroacetyl-CoA TE''' from ''Streptomyces cattleya'' hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate<ref>PMID:20836570</ref>.<br />
+*  '''Ubiquitin TE''' or '''ubiquitin carboxyl-terminal hydrolase''' (USP) removes conjugated ubiquitin (UB) from proteins thus regulating protein level by preventing their degradation.  USP hydrolyze the peptide bond at the C-terminal glycine of ubiquitin.  The USPs are involved in the processing of poly-UB precursors and of ubiquitinated proteins<ref>PMID:24190967</ref>.  USP contains catalytic domain surrounded several domains:  Ub-like (UBL); Ub-associated (UBA); zinc finger-Ub-specific protease domain (UBP or DUSP); TRAF homology domain.
-<!--
+* '''USP-L1, USP25''' hydrolyze C-terminal adducts of UB.<br />
-Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+* '''USP-L3''' hydrolyzes C-terminal adducts of UB and NEDD8.<br />
-Or use the four-green-boxes-button to insert scrollable text adjacent
+* '''USP5''' cleaves multiubiquitin polymers.<br />
-to a Jmol applet. Check out the other buttons as well!
+* '''USP6''' has ATP-independent isopeptidase activity.<br />
--->
+* '''USP7, USP4, USP13, USP15''' deubiquitinate several proteins.<br />
-'''Thioesterase''' (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group.  TEs are substrate-specific.  Palmitoyl protein TE removes fatty acids like palmitate from modified cysteine residues during lysosomal degradation.  4-hydroxybenzoyl-CoA TE converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA.  Acyl-CoA TE hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism.   Fluoroacetyl-CoA TE from ''Streptomyces cattleya'' hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate.  Ubiquitin TE removes conjugated ubiquitin from proteins thus regulating protein level by preventing their degradation.
+* '''USP8''' removes conjugated ubiquitin from proteins thus preventing protein degradation.  USP8 is involved in cell proliferation and is active in the M phase of proliferation.<br />
+* '''USP11, USP14''' are proteasome-associated.<br />
+* '''USP12''' stabilizes T-cell complexes<ref>PMID:26811477</ref>.<br />
+* '''USP16, USP21''' deubiquitinate histone H2A.<br />
+* '''USP18''' is a down regulator of the type I interferon signaling pathway<ref>PMID:23700969</ref>.<br />
+* '''USP28''' deubiquitinates proteins of the DNA damage pathway.<br />
+* '''USP33''' regulates centrosome duplication.<br />
+* '''USP37''' deubiquitinates cyclin A.<br />
+* '''USP46''' deubiquitinates AMPA receptor<ref>PMID:26077708</ref>.<br />
+== Disease ==
+Mutations in palmiotoyl protein TE cause neuronal ceroid lipocfuscinosis<ref>PMID:7637805</ref><ref>PMID:11506414</ref>.
+== Structural highlights ==
+<scene name='48/489265/Cv/7'>Human ubiquitin esterase 2 complex with ubiquitin and zinc+2 ion</scene>. Ubiquitin thioesterase 2 active site contains the <scene name='48/489265/Cv/8'>catalytic triad Cys-His-Asn and the oxyanion hole Asn</scene>. The metal-binding enzyme contains a <scene name='48/489265/Cv/9'>Zn+2 ion which coordinates to 4 Cys residues</scene>. The <scene name='48/489265/Cv/10'>ubiquitin coordinates to the thioesterase via residues in all thioesterase domains: finger, palm and thumb</scene><ref>PMID:16905103</ref>.
 ==3D structures of thioesterase==
+[[Thioesterase 3D structures]]
+</StructureSection>
-'''Maristoyl-ACP-specific TE'''
+== References ==
+<references/>
-[[1tht]] – TE – Vibrio harveyi
+[[Category:Topic Page]]
-'''4-hydroxybenzoyl-CoA TE'''
-[[1bvq]] – PsTE – ''Pseudomonas''<br />
-[[1lo7]] – PsTE + 4-hydroxyphenyl CoA<br />
-[[1lo9]] - PsTE (mutant) + 4-hydroxybenzoyl CoA<br />
-[[1lo8]] - PsTE + 4-hydroxybenzyl CoA<br />
-[[1q4s]] - ArTE + 4-hydroxybenzoate – '''Arthrobacte''r'<br />
-[[1q4t]] - ArTE + 4-hydroxyphenyl CoA<br />
-[[1q4u]] - ArTE + 4-hydroxybenzyl CoA<br />
-[[3r32]], [[3r35]], [[3r37]], [[3r38]], [[3r3c]], [[3r3d]], [[3r3f]] - ArTE (mutant) + 4-hydroxyphenacyl CoA<br />
-[[3r3a]] - ArTE (mutant) + 4-hydroxybenzoate<br />
-[[3r34]] - ArTE (mutant) + CoA<br />
-'''Palmitoyl protein TE'''
-[[1eh5]] – bTE1 + Palmitate – bovine<br />
-[[1ei9]] – bTE1<br />
-[[1exw]] – bTE1 + hexadecylsulfonyl fluoride<br />
-[[1pja]] – hTEII – human<br />
-[[3gro]] - hTEI
-'''Acyl-CoA TE'''
-[[1c8u]] – EcTEII – ''Escherichia coli''<br />
-[[1ivn]] – EcTEI<br />
-[[1jrl]] – EcTEI (mutant) <br />
-[[1j00]] – EcTEI + diethyl phosphono derivative<br />
-[[1v2g]], [[1u8u]] - EcTEI + octanoic acid<br />
-[[2v1o]] – mTE7 hotdog domain – mouse<br />
-[[2q2b]] – mTE7 C terminal<br />
-[[3hlk]] – hTE2<br />
-[[3k2i]] – hTE4<br />
-[[2qq2]] - hTE7 C terminal<br />
-[[3fo5]] – hTE11 START domain<br />
-[[3b7k]] – hTE12<br />
-[[3rd7]] – TE – ''Mycobacterium avium''<br />
-[[3u0a]] – TEII – ''Mycobacterium marinum''<br />
-[[1tbu]] – TE N terminal (peroximal) – yeast
-'''Acyl protein TE'''
-[[1fj2]] – EcTEI
-'''Acyl-ACP TE'''
-[[2ess]] – TE – ''Bacterioides thetaiotaomicron''
-'''Fluoroacetyl-CoA TE'''
-[[3kuv]], [[3kuw]], [[3kvi]] – ScTE (mutant) + acetate derivative – ''Streptomyces cattleya''<br />
-[[3kv7]], [[3kv8]], [[3p2r]], [[3p2s]] – ScTE + acetate derivative<br />
-[[3kvu]] – ScTE + acetyl-CoA<br />
-[[3kvz]] – ScTE + FAcOPan<br />
-[[3kx7]], [[3fx8]], [[3p2q]] – ScTE <br />
-[[3p3f]] – ScTE (mutant) <br />
-[[3p3i]] - ScTE (mutant) + acetate derivative + CoA<br />
-'''Ubiquitin TE'''
-[[2kzr]] – mTE UBX-like domain – NMR<br />
-[[4dhi]] – CeTE + ubiquitin-conjugating enzyme E2 – ''Caenorhabditis elegans''<br />
-[[4dhj]], [[4dhz]] – CeTE + ubiquitin-conjugating enzyme E2 + ubiquitin + ubiquitin aldehyde
-'''RedJ TE'''
-[[3qmv]], [[3qmw]] – TE –'' Streptomyces coelicolor''
-[[2av9 ]]– TE – ''Pseudomonas aeruginosa''