Thioesterase
FunctionThioesterase (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group. TEs are substrate-specific.
DiseaseMutations 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]. |
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3D structures of thioesterase3D structures of thioesterase
Updated on 12-September-2016
5fwi]] – hUSP catalytic + UBL domains 1+2
- Ubiquitin thioesterase 7 complexes
- 1nbf – hUSP catalytic domain + Ub aldehyde
- 5jtj – hUSP catalytic domain + Ub
- 1yy6 – hUSP N terminal domain + EBNA1 peptide
- 2xxn – hUSP TRAF domain + VIRF-4 peptide
- 3mqr – hUSP TRAF domain + HDMX peptide
- 3mqs – hUSP TRAF domain + HDM2 peptide
- 4jjq – hUSP TRAF domain + E2 peptide
- 4kg9 – hUSP TRAF domain + MCM-BP peptide
- 4ysi – hUSP TRAF domain + peptide
- 4yoc – hUSP residues 560-1102 + DNA methyl transferase
- 5c6d – hUSP residues 561-881 + UHRF1
- 5c56 – hUSP residues 560-1102 + Ub E3 ligase Icp0444w
- 1nbf – hUSP catalytic domain + Ub aldehyde
- Ubiquitin thioesterase 8
- Ubiquitin thioesterase 8 complexes
- Ubiquitin thioesterase 11
- Ubiquitin thioesterase 12
- Ubiquitin thioesterase 13
- Ubiquitin thioesterase 14
- Ubiquitin thioesterase 15
- Ubiquitin thioesterase 16
- 2i50 – hUSP zinc finger domain - NMR
- 2i50 – hUSP zinc finger domain - NMR
- Ubiquitin thioesterase 18
- 5cht – hUSP
- 5cht – hUSP
- Ubiquitin thioesterase 21
- Ubiquitin thioesterase 25
- 1vdl – mUSP catalytic domain
- 1vdl – mUSP catalytic domain
- Ubiquitin thioesterase 28
- Ubiquitin thioesterase 33
- 2uzg – hUSP zinc finger domain - NMR
- 2uzg – hUSP zinc finger domain - NMR
- Ubiquitin thioesterase 37
- Ubiquitin thioesterase 38
- 4rxx – hUSP N terminal
- 4rxx – hUSP N terminal
- Ubiquitin thioesterase 46
- Ubiquitin thioesterase Cyld
- 2vhf – hUSP USP domain
- 2vhf – hUSP USP domain
- Ubiquitin thioesterase L1
- Ubiquitin thioesterase L3
- Ubiquitin thioesterase L5
- 3ris – hUSP catalytic domain
- 3rii, 3a7s – hUSP catalytic domain (mutant)
- 3tb3 – hUSP UCH domain (mutant)
- 3ihr – hUSP-L5 (mutant)
- 4uel – hUSP-L5 + polyUb + proteasomal Ub receptor Deubad domain
- 4uem – hUSP-L5 + proteasomal Ub receptor Deubad domain
- 4wlq – mUSP-L5 + proteasomal Ub receptor C terminal
- 4wlr – mUSP-L5 + polyUb + proteasomal Ub receptor C terminal
- 4uf5, 4wlp – hUSP-L5 + nuclear factor Deubad domain
- 4uf6 – hUSP-L5 + polyUb + nuclear factor Deubad domain
- 3ris – hUSP catalytic domain
- Ubiquitin thioesterase ZranB1
- Ubiquitin thioesterase OTUB1
- 3von – hUSP + E2
- 4ddg, 4ddi – hUSP + Ub
- 4i6l – hUSP (mutant) + Ub
- 4dhz, 4ldt – hUSP + E2 + Ub
- 4boq - hUSP OTU domain
- 4boz - hUSP OTU domain (mutant) + Ub
- 4bos - hUSP OTU domain (mutant) + Ub + OTUD2 peptide
- 4fjv - hUSP OTUB2 + Ub
- 4dhj – nUSP + E2 + Ub - nematode
- 4dhi – nUSP + E2
- 2kzr – mUSP UBX-like domain – NMR
- 4kdi, 4kdl – yUSP UBX-like domain + transitional endoplasmic reticulum ATPase
- 3by4, 3c0r - yUSP OTU domain + Ub
- 3von – hUSP + E2
- Ubiquitin thioesterase
- 3znh – USP OTU domain + Ub – Crimean-Congo hemorrhagic fever virus
- 3znh – USP OTU domain + Ub – Crimean-Congo hemorrhagic fever virus
- Pseudomonas aeruginosa TE
ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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