Thioesterase: Difference between revisions

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== Structural highlights ==
== 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>.
<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>
</StructureSection>
==3D structures of thioesterase==
==3D structures of thioesterase==
Line 53: Line 56:
**[[3r34]] - ArTE (mutant) + CoA<br />
**[[3r34]] - ArTE (mutant) + CoA<br />
**[[6fdg]] – SaTE  – ''Staphylococcus aureus''<br />
**[[6fdg]] – SaTE  – ''Staphylococcus aureus''<br />
**[[5wh9]] – TE  – ''Bacillus halodurans''<br />


*Palmitoyl protein thioesterase
*Palmitoyl protein thioesterase


**[[3gro]] - hTEI - human<br />
**[[1pja]] – hTEII <br />
**[[1eh5]] – bTE1 + Palmitate – bovine<br />
**[[1eh5]] – bTE1 + Palmitate – bovine<br />
**[[1ei9]] – bTE1<br />
**[[1ei9]] – bTE1<br />
**[[1exw]] – bTE1 + hexadecylsulfonyl fluoride<br />
**[[1exw]] – bTE1 + hexadecylsulfonyl fluoride<br />
**[[1pja]] – hTEII – human<br />
**[[3gro]] - hTEI


*Acyl-CoA thioesterase
*Acyl-CoA thioesterase or acyl-CoA thioester hydrolase


**[[3hlk]] – hTE2<br />
**[[3k2i]] – hTE4<br />
**[[2qq2]] - hTE7 C terminal<br />
**[[3fo5]] – hTE11 START domain<br />
**[[3b7k]], [[4moc]] – hTE12<br />
**[[4mob]] – hTE12 + ADP<br />
**[[2v1o]] – mTE7 hotdog domain – mouse<br />
**[[2q2b]] – mTE7 C terminal<br />
**[[6vfy]] – mTE7 42-367 + acyl-CoA TE hydrolase + CoA<br />
**[[1tbu]] – TEI N terminal (peroximal) – yeast<br />
**[[2pzh]] - TE - ''Helicobacter pylori''<br />
**[[2pzh]] - TE - ''Helicobacter pylori''<br />
**[[3rd7]] – TE – ''Mycobacterium avium''<br />
**[[3rd7]] – TE – ''Mycobacterium avium''<br />
**[[5v3a]] – NmTE  + CoA + GDP – ''Neisseria meningitis''<br />
**[[5t02]] – NmTE (mutant)  + CoA + GDP <br />
**[[5hz4]], [[5hwf]], [[5egk]] – SaTE (mutant)  – ''Staphylococcus aureus''<br />
**[[5hz4]], [[5hwf]], [[5egk]] – SaTE (mutant)  – ''Staphylococcus aureus''<br />
**[[4egj]] – SaTE + CoA<br />
**[[4egj]] – SaTE + CoA<br />
Line 75: Line 87:
**[[1v2g]], [[1u8u]] - EcTEI + octanoic acid<br />
**[[1v2g]], [[1u8u]] - EcTEI + octanoic acid<br />
**[[5tid]], [[5tie]], [[5tif]] - EcTEI (mutant) + octanoic acid<br />
**[[5tid]], [[5tie]], [[5tif]] - EcTEI (mutant) + octanoic acid<br />
**[[1tbu]] – TEI N terminal (peroximal) – yeast<br />
**[[5tid]], [[5tie]], [[5tif]] - EcTEI (mutant) + octanoic acid<br />
**[[5t06]] - EcTEI (mutant) + hexanoyl-CoA<br />
**[[5t07]] - EcTEI (mutant) + decanoyl-CoA<br />
**[[1c8u]] – EcTEII <br />
**[[1c8u]] – EcTEII <br />
**[[3u0a]] – TEII – ''Mycobacterium marinum''<br />
**[[3u0a]] – TEII – ''Mycobacterium marinum''<br />
**[[4qfw]] – YpTE II – ''Yersinia pestis''<br />
**[[4qfw]] – YpTE II – ''Yersinia pestis''<br />
**[[4r4u]] – YpTE II + CoA<br />
**[[4r4u]] – YpTE II + CoA<br />
**[[3hlk]] – hTE2<br />
**[[5szv]], [[5szu]] – NmTE  + CoA – ''Neisseria meningitis''<br />
**[[3k2i]] – hTE4<br />
**[[5szz]], [[5szy]] – NmTE  + CoA + GDP<br />
**[[2qq2]] - hTE7 C terminal<br />
**[[5v3a]] – NmTE  + CoA + GDP <br />
**[[2v1o]] – mTE7 hotdog domain – mouse<br />
**[[5t02]] – NmTE (mutant)  + CoA + GDP <br />
**[[2q2b]] – mTE7 C terminal<br />
**[[3fo5]] – hTE11 START domain<br />
**[[3b7k]], [[4moc]] – hTE12<br />
**[[4mob]] – hTE12 + ADP<br />


*Acyl protein thioesterase
*Acyl protein thioesterase


**[[5sym]], [[6bje]] – hTE 1 + inhibitor<br />
**[[6qgs]] – hTE 1 + palmitate<br />
**[[6qgq]], [[6qgo]], [[6qgn]] – hTE 1 (mutant) + palmitate<br />
**[[5syn]] – hTE 2 + inhibitor<br />
**[[6avy]] – TE 2 - maize<br />
**[[1fj2]] – EcTEI<br />
**[[1fj2]] – EcTEI<br />
**[[6avy]] – TE 2 - maize<br />
**[[5sym]] – hTE 1 + inhibitor<br />
**[[5syn]] – hTE 2 + inhibitor<br />


*Acyl-ACP thioesterase
*Acyl-ACP thioesterase
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*Ubiquitin thioesterase 2
*Ubiquitin thioesterase 2


**[[2zfy]] – hUSP – human  <BR />
**[[2zfy]] – hUSP <BR />
**[[2hd5]], [[3nhe]], [[3v6c]], [[3v6e]] – hUSP + Ub  <BR />
**[[2hd5]], [[3nhe]], [[3v6c]], [[3v6e]] – hUSP + Ub  <BR />
**[[1tff]] – hUSP (mutant)  <BR />
**[[1tff]] – hUSP (mutant)  <BR />
**[[2ibi]] – hUSP (mutant) + Ub <BR />
**[[2ibi]], [[5xve]] – hUSP (mutant) + Ub <BR />
**[[5xu8]] – hUSP + Ub + thioguanine <BR />


*Ubiquitin thioesterase 3
*Ubiquitin thioesterase 3
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**[[2g43]], [[6dxh]], [[6dxt]] – hUSP zinc finger USP domain<br />
**[[2g43]], [[6dxh]], [[6dxt]] – hUSP zinc finger USP domain<br />
**[[2g45]] – hUSP zinc finger USP domain + Ub<br />
**[[2g45]] – hUSP zinc finger USP domain + Ub<br />
**[[6p9g]], [[6nft]] – hUSP zinc finger USP domain + quinazoline derivative<br />
**[[3ihp]] – hUSP + Ub  <BR />
**[[3ihp]] – hUSP + Ub  <BR />


Line 178: Line 192:


**[[1nbf]] – hUSP catalytic domain + Ub aldehyde<br />
**[[1nbf]] – hUSP catalytic domain + Ub aldehyde<br />
**[[5jtj]] – hUSP catalytic domain + polyubiquitin <br />
**[[5jtj]], [[5jtv]] – hUSP catalytic domain + polyubiquitin <br />
**[[5whc]], [[5n9r]], [[5n9t]], [[5uqv]], [[5uqx]], [[6f5h]] – hUSP catalytic domain + inhibitor<br />
**[[5whc]], [[5n9r]], [[5n9t]], [[5uqv]], [[5uqx]], [[6f5h]], [[5vsk]], [[5vsb]], [[5vs6]], [[5ngf]], [[5nge]] – hUSP catalytic domain + inhibitor<br />
**[[5kyc]], [[5kyd]], [[5kye]], [[5kyf]] – hUSP catalytic domain (mutant) + polyubiquitin <br />
**[[5kyc]], [[5kyd]], [[5kye]], [[5kyf]] – hUSP catalytic domain (mutant) + polyubiquitin <br />
**[[1yy6]] – hUSP TRAF domain + EBNA1 peptide<br />
**[[1yy6]] – hUSP TRAF domain + EBNA1 peptide<br />
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**[[2fop]] – hUSP TRAF domain + MDM2 peptide<br />
**[[2fop]] – hUSP TRAF domain + MDM2 peptide<br />
**[[4jjq]] – hUSP TRAF domain + E2 peptide<br />
**[[4jjq]] – hUSP TRAF domain + E2 peptide<br />
**[[5gg4]] – hUSP TRAF domain + E3 peptide<br />
**[[4kg9]] – hUSP TRAF domain + MCM-BP peptide<br />
**[[4kg9]] – hUSP TRAF domain + MCM-BP peptide<br />
**[[4ysi]], [[2foj]], [[2foo]] – hUSP TRAF domain + peptide<br />
**[[4ysi]], [[2foj]], [[2foo]] – hUSP TRAF domain + peptide<br />
**[[4yoc]], [[4z96]], [[4z97]] – hUSP residues 560-1102 + DNMT1<br />
**[[4yoc]], [[4z96]], [[4z97]] – hUSP residues 560-1102 + DNMT1<br />
**[[5c6d]] – hUSP residues 561-881 + UHRF1<br />
**[[5c6d]] – hUSP UBL2 domain + UHRF1<br />
**[[5c56]] – hUSP residues 560-1102 + Ub E3 ligase Icp0444w<br />
**[[5c56]] – hUSP residues 560-1102 + Ub E3 ligase Icp0444w<br />


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**[[2a9u]] – hUSP N terminal domain <br />
**[[2a9u]] – hUSP N terminal domain <br />
**[[2gfo]] – hUSP catalytic domain <br />
**[[2gfo]] – hUSP catalytic domain <br />
**[[3n3k]] – hUSP catalytic domain + ubiqitin<br />


*Ubiquitin thioesterase 8 complexes
*Ubiquitin thioesterase 8 complexes


**[[2gwf]] – hUSP rhodanase domain + ring finger protein 41 USP8 interaction domain<br />
**[[2gwf]] – hUSP rhodanase domain + ring finger protein 41 USP8 interaction domain<br />
**[[3mhh]], [[3m99]], [[4fip]], [[4fjc]], [[4f5k]], [[4fk5]] – yUSP + SUS1 + SGF11 +SGF73 <br />
**[[3n3k]] – hUSP catalytic domain + Ub<br />
**[[3mhs]] – yUSP + SUS1 + SGF11 +SGF73 + Ub<br />
**[[3mhh]], [[3m99]], [[4fip]], [[4fjc]], [[4f5k]], [[4fk5]], [[4wa6]] – yUSP + SUS1 + SGF11 +SGF73 <br />
**[[3mhs]], [[6aqr]] – yUSP + SUS1 + SGF11 +SGF73 + Ub<br />
**[[4zux]] – yUSP + SUS1 + SGF11 +SGF73 + Ub + Histones H3,2, H4, H2A, H2B + DNA<br />
**[[4zux]] – yUSP + SUS1 + SGF11 +SGF73 + Ub + Histones H3,2, H4, H2A, H2B + DNA<br />
**[[3n3k]] – hUSP catalytic domain + Ub<br />
 


*Ubiquitin thioesterase 9
*Ubiquitin thioesterase 9
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**[[4mel]] – hUSP DUSP+UBL domains <br />
**[[4mel]] – hUSP DUSP+UBL domains <br />
**[[5ok6]] – hUSP DUSP+UBL domains + peptide<br />
**[[4mem]] – rUSP DUSP+UBL domains - rat<br />
**[[4mem]] – rUSP DUSP+UBL domains - rat<br />


Line 231: Line 247:
*Ubiquitin thioesterase 14
*Ubiquitin thioesterase 14


**[[2ayn]] – hUSP catalytic domain<br />
**[[2ayo]] – hUSP catalytic domain + Ub aldehyde<br />
**[[6iin]], [[6iim]], [[6iil]], [[6iik]] – hUSP catalytic domain + inhibitor<br />
**[[5gjq]] – hUSP in proteasome – Cryo EM<br />
**[[1wiv]] – AtUSP UBA domain - NMR<br />
**[[1wgg]] – mUSP N terminal domain - NMR<br />
**[[1wgg]] – mUSP N terminal domain - NMR<br />
**[[2ayn]] – hUSP<br />
**[[2ayo]] – hUSP + Ub aldehyde<br />
**[[1wiv]] – AtUSP UBA domain - NMR<br />
**[[5gjq]] – hUSP in proteasome – Cryo EM<br />


*Ubiquitin thioesterase 15
*Ubiquitin thioesterase 15; domains – DUSP 1-133; UBL 134-223; catalytic 255-439+757-919


**[[3lmn]] – hUSP DUSP domain  <BR />
**[[3lmn]] – hUSP DUSP domain  <BR />
**[[1w6v]] – hUSP DUSP domain - NMR<br />
**[[3ppa]], [[3pv1]], [[3t9l]], [[4a3o]], [[4a3p]] – hUSP DUSP+UBL domains <br />
**[[3ppa]], [[3pv1]], [[3t9l]], [[4a3o]], [[4a3p]] – hUSP DUSP+UBL domains <br />
**[[1w6v]] – hUSP DUSP domain - NMR<br />
**[[6dj9]] – hUSP DUSP domain + Ub<BR />  
**[[5jjw]] – hUSP catalytic domain + SART HAT domain<br />
**[[6gha]] – hUSP catalytic domain <BR />
**[[5ctr]] – hUSP DUSP+UBL domains + SART HAT domain <br />
**[[5ctr]], [[5jjw]] – hUSP DUSP+UBL domains + SART HAT domain <br />
**[[6ml1]], [[6crn]], [[6cpm]] – hUSP catalytic domain + Ub <BR />
**[[6gh9]] – hUSP catalytic domain + quinone derivative <BR />


*Ubiquitin thioesterase 16
*Ubiquitin thioesterase 16
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*Ubiquitin thioesterase 18
*Ubiquitin thioesterase 18


**[[5cht]] – hUSP   <BR />
**[[5cht]] – mUSP  <BR />
**[[5chv]] – mUSP + Ub-like  <BR />
 
*USP 20
 
**[[6kcz]] – hUSP zinc finger + UBP domains - NMR  <BR />


*Ubiquitin thioesterase 21
*Ubiquitin thioesterase 21
Line 260: Line 285:
*Ubiquitin thioesterase 25
*Ubiquitin thioesterase 25


**[[5o71]] – hUSP <BR />
**[[6hem]], [[6h4k]] – hUSP C terminal  <BR />
**[[6hel]], [[6h4j]] – hUSP residues 157-714 <BR />
**[[1vdl]] – mUSP catalytic domain <br />
**[[1vdl]] – mUSP catalytic domain <br />


*Ubiquitin thioesterase 28
*Ubiquitin thioesterase 28;; domains – catalytic 149-399


**[[6hej]] – hUSP residues 149-703<BR />
**[[2lva]], [[2muu]], [[2mux]] – hUSP N terminal - NMR  <BR />
**[[2lva]], [[2muu]], [[2mux]] – hUSP N terminal - NMR  <BR />
**[[6h4i]] – hUSP catalytic domain <BR />
**[[6heh]] – hUSP catalytic domain (mutant)<BR />
**[[6hek]] – hUSP residues 149-703 + Ub  <BR />
**[[6hei]], [[6h4h]] – hUSP catalytic domain (mutant) + Ub  <BR />


*Ubiquitin thioesterase 30
*Ubiquitin thioesterase 30
Line 291: Line 324:
*Ubiquitin thioesterase 46
*Ubiquitin thioesterase 46


**[[5cvm]] – hUSP + Ub  <BR />
**[[5cvm]], [[5l8h]] – hUSP + Ub  <BR />
**[[5cvn]], [[5cvo]] – hUSP + WD repeat-containing protein + Ub<br />
**[[5cvn]], [[5cvo]] – hUSP + WDR48 + Ub<br />
**[[6jlq]] – hUSP + WDR48 + WDR20<br />


*Ubiquitin thioesterase Cyld
*Ubiquitin thioesterase Cyld
Line 310: Line 344:
**[[1uch]] – hUSP-L3  <br />
**[[1uch]] – hUSP-L3  <br />
**[[1xd3]] – hUSP-L3 + UBC<br />
**[[1xd3]] – hUSP-L3 + UBC<br />
**[[6isu]] – hUSP-L3 + Ub <br />
**[[2we6]] – PfUSP-L3 – ''Plasmodium falciparum''<br />
**[[2we6]] – PfUSP-L3 – ''Plasmodium falciparum''<br />
**[[2wdt]] – PfUSP-L3 + Ub <br />
**[[2wdt]] – PfUSP-L3 + Ub <br />
Line 321: Line 356:
**[[4uel]] – hUSP-L5 + polyUb + proteasomal Ub receptor Deubad domain  <br />
**[[4uel]] – hUSP-L5 + polyUb + proteasomal Ub receptor Deubad domain  <br />
**[[4uem]] – hUSP-L5 + proteasomal Ub receptor Deubad domain  <br />
**[[4uem]] – hUSP-L5 + proteasomal Ub receptor Deubad domain  <br />
**[[4uf5]], [[4wlp]] – hUSP-L5 + nuclear factor Deubad domain  <br />
**[[4uf6]] – hUSP-L5 + polyUb + nuclear factor Deubad domain  <br />
**[[4wlq]] – mUSP-L5 + proteasomal Ub receptor C terminal  <br />
**[[4wlq]] – mUSP-L5 + proteasomal Ub receptor C terminal  <br />
**[[4wlr]] – mUSP-L5 + polyUb + proteasomal Ub receptor C terminal  <br />
**[[4wlr]] – mUSP-L5 + polyUb + proteasomal Ub receptor C terminal  <br />
**[[4uf5]], [[4wlp]] – hUSP-L5 + nuclear factor Deubad domain  <br />
**[[4uf6]] – hUSP-L5 + polyUb + nuclear factor Deubad domain  <br />


*Ubiquitin thioesterase ZranB1
*Ubiquitin thioesterase ZranB1
Line 340: Line 375:
**[[4boz]] - hUSP OTU domain (mutant) + Ub <BR />
**[[4boz]] - hUSP OTU domain (mutant) + Ub <BR />
**[[4bos]] - hUSP OTU domain (mutant) + Ub + OTUD2 peptide<BR />
**[[4bos]] - hUSP OTU domain (mutant) + Ub + OTUD2 peptide<BR />
**[[4fjv]] - hUSP OTUB2 + Ub <BR />
**[[4dhj]] – nUSP + E2 + Ub - nematode<BR />
**[[4dhi]] – nUSP + E2 <BR />
**[[4dhi]] – nUSP + E2 <BR />
**[[2kzr]] – mUSP UBX-like domain – NMR<br />
**[[2kzr]] – mUSP UBX-like domain – NMR<br />
**[[4dhj]] – nUSP + E2 + Ub - nematode<BR />
**[[4kdi]], [[4kdl]] – yUSP UBX-like domain + transitional endoplasmic reticulum ATPase<br />
**[[4kdi]], [[4kdl]] – yUSP UBX-like domain + transitional endoplasmic reticulum ATPase<br />
**[[3by4]], [[3c0r]] - yUSP OTU domain + Ub<BR />
**[[3by4]], [[3c0r]] - yUSP OTU domain + Ub<BR />
*USP OTUB2
**[[5qiz]], [[5qiy]], [[5qix]], [[5qiw]], [[5qiu]], [[5qiv]], [[5qis]], [[5qit]], [[5qio]], [[5qip]], [[5qiq]], [[5qir]] – hUSP OTUB2 + ligand <BR />
**[[4fjv]] - hUSP OTUB2 + Ub <BR />
*USP OTULIN; Domains – OUT 80-345
**[[6i9c]] – hUSP OTU domain (mutant) <BR />
**[[5oe7]] – hUSP OUT domain + Ub <BR />
**[[6sak]] – hUSP OUT domain (mutant) + sorting nexin-27<BR />


*Ubiquitin thioesterase  
*Ubiquitin thioesterase  
Line 362: Line 407:
**[[5vpj]] – TE – ''Actinomadura verrucosospora''<br />
**[[5vpj]] – TE – ''Actinomadura verrucosospora''<br />
**[[5dio]], [[5byu]] – TE – ''Legionella pneumophila''<br />
**[[5dio]], [[5byu]] – TE – ''Legionella pneumophila''<br />
**[[6fvj]] – TE – ''Mycobacterium tuberculosis''<br />


}}
}}

Revision as of 14:48, 18 February 2020

Function

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[1]. For details see Palmitoyl protein thioesterase.
  • 4-hydroxybenzoyl-CoA TE converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA[2].
  • Acyl-CoA TE hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism[3]. See also YbgC.
  • Fluoroacetyl-CoA TE from Streptomyces cattleya hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate[4].
  • 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[5]. 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.
  • USP-L3 hydrolyzes C-terminal adducts of UB and NEDD8.
  • USP5 cleaves multiubiquitin polymers.
  • USP6 has ATP-independent isopeptidase activity.
  • USP7, USP4, USP13, USP15 deubiquitinate several proteins.
  • 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.
  • USP11, USP14 are proteasome-associated.
  • USP12 stabilizes T-cell complexes[6].
  • USP16, USP21 deubiquitinate histone H2A.
  • USP18 is a down regulator of the type I interferon signaling pathway[7].
  • USP28 deubiquitinates proteins of the DNA damage pathway.
  • USP33 regulates centrosome duplication.
  • USP37 deubiquitinates cyclin A.
  • USP46 deubiquitinates AMPA receptor[8].

Disease

Mutations in palmiotoyl protein TE cause neuronal ceroid lipocfuscinosis[9][10].

Structural highlights

. Ubiquitin thioesterase 2 active site contains the . The metal-binding enzyme contains a . The [11].

3D structures of thioesterase

Thioesterase 3D structures


Human ubiquitin esterase 2 (deepskyblue) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code 2hd5).

Drag the structure with the mouse to rotate

3D structures of thioesterase3D structures of thioesterase

Updated on 18-February-2020

ReferencesReferences

  1. ↑ Cho S, Dawson G. Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells. J Neurochem. 2000 Apr;74(4):1478-88. PMID:10737604
  2. ↑ Zhuang Z, Gartemann KH, Eichenlaub R, Dunaway-Mariano D. Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU. Appl Environ Microbiol. 2003 May;69(5):2707-11. PMID:12732540
  3. ↑ Hunt MC, Alexson SE. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. PMID:11755680
  4. ↑ Weeks AM, Coyle SM, Jinek M, Doudna JA, Chang MC. Structural and Biochemical Studies of a Fluoroacetyl-CoA-Specific Thioesterase Reveal a Molecular Basis for Fluorine Selectivity. Biochemistry. 2010 Oct 11. PMID:20836570 doi:10.1021/bi101102u
  5. ↑ Jagannathan M, Nguyen T, Gallo D, Luthra N, Brown GW, Saridakis V, Frappier L. A role for USP7 in DNA replication. Mol Cell Biol. 2014 Jan;34(1):132-45. doi: 10.1128/MCB.00639-13. Epub 2013 Nov 4. PMID:24190967 doi:http://dx.doi.org/10.1128/MCB.00639-13
  6. ↑ Jahan AS, Lestra M, Swee LK, Fan Y, Lamers MM, Tafesse FG, Theile CS, Spooner E, Bruzzone R, Ploegh HL, Sanyal S. Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling. Proc Natl Acad Sci U S A. 2016 Feb 9;113(6):E705-14. doi:, 10.1073/pnas.1521763113. Epub 2016 Jan 25. PMID:26811477 doi:http://dx.doi.org/10.1073/pnas.1521763113
  7. ↑ Malhotra S, Morcillo-Suarez C, Nurtdinov R, Rio J, Sarro E, Moreno M, Castillo J, Navarro A, Montalban X, Comabella M. Roles of the ubiquitin peptidase USP18 in multiple sclerosis and the response to interferon-beta treatment. Eur J Neurol. 2013 Oct;20(10):1390-7. doi: 10.1111/ene.12193. Epub 2013 May 22. PMID:23700969 doi:http://dx.doi.org/10.1111/ene.12193
  8. ↑ Huo Y, Khatri N, Hou Q, Gilbert J, Wang G, Man HY. The deubiquitinating enzyme USP46 regulates AMPA receptor ubiquitination and trafficking. J Neurochem. 2015 Sep;134(6):1067-80. doi: 10.1111/jnc.13194. Epub 2015 Jul 16. PMID:26077708 doi:http://dx.doi.org/10.1111/jnc.13194
  9. ↑ Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. PMID:7637805 doi:http://dx.doi.org/10.1038/376584a0
  10. ↑ van Diggelen OP, Thobois S, Tilikete C, Zabot MT, Keulemans JL, van Bunderen PA, Taschner PE, Losekoot M, Voznyi YV. Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase deficiency: first adult-onset patients of a childhood disease. Ann Neurol. 2001 Aug;50(2):269-72. PMID:11506414
  11. ↑ Renatus M, Parrado SG, D'Arcy A, Eidhoff U, Gerhartz B, Hassiepen U, Pierrat B, Riedl R, Vinzenz D, Worpenberg S, Kroemer M. Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure. 2006 Aug;14(8):1293-302. PMID:16905103 doi:10.1016/j.str.2006.06.012

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