Thioesterase: Difference between revisions

Revision as of 11:50, 11 September 2016

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); TRF homology domain.

USP-L1, USP25 hydrolyze C-terminal adducts of UB.
USP-L3 hydrolyze 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.
USP16, USP21 deubiquitinate histone H2A.
USP28 deubiquitinates proteins of the DNA damage pathway.
USP33 regulates centrosome duplication.
USP37 deubiquitinates cyclin A.

Disease

Mutations in palmiotoyl protein TE cause neuronal ceroid lipocfuscinosis^[6]^[7].

Structural highlights

Ubiquitin thioesterase 2 active site contains the catalytic triad Cys-His-Asn and the oxyanion hole Asn. The metal-binding enzyme contains a Zn+2 ion which coordinates to 4 Cys residues. The ubiquitin coordinates to the thioesterase via residues in all thioesterase domains: finger, palm and thumb^[8].

Human ubiquitin esterase 2 (grey) 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 11-September-2016

Maristoyl-ACP-specific thioesterase
- 1tht – TE – Vibrio harveyi
4-hydroxybenzoyl-CoA thioesterase
- 1bvq – PsTE – Pseudomonas
- 1lo7 – PsTE + 4-hydroxyphenyl CoA
- 1lo9 - PsTE (mutant) + 4-hydroxybenzoyl CoA
- 1lo8 - PsTE + 4-hydroxybenzyl CoA
- 1q4s - ArTE + 4-hydroxybenzoate – 'Arthrobacter'
- 1q4t - ArTE + 4-hydroxyphenyl CoA
- 1q4u - ArTE + 4-hydroxybenzyl CoA
- 3r32, 3r35, 3r37, 3r38, 3r3b, 3r3c, 3r3d, 3r3f, 3tea - ArTE (mutant) + 4-hydroxyphenacyl CoA
- 3r36 - ArTE (mutant) + 4-hydroxybenzoate
- 3r3a - ArTE (mutant) + 4-hydroxybenzoate + CoA
- 3r34 - ArTE (mutant) + CoA
Palmitoyl protein thioesterase
- 1eh5 – bTE1 + Palmitate – bovine
- 1ei9 – bTE1
- 1exw – bTE1 + hexadecylsulfonyl fluoride
- 1pja – hTEII – human
- 3gro - hTEI
Acyl-CoA thioesterase
- 1c8u – EcTEII – Escherichia coli
- 1ivn – EcTEI
- 1jrl – EcTEI (mutant)
- 1j00 – EcTEI + diethyl phosphono derivative
- 1v2g, 1u8u - EcTEI + octanoic acid
- 2v1o – mTE7 hotdog domain – mouse
- 2q2b – mTE7 C terminal
- 2pzh - TE - Helicobacter pylori
- 3hlk – hTE2
- 3k2i – hTE4
- 2qq2 - hTE7 C terminal
- 3fo5 – hTE11 START domain
- 3b7k, 4moc – hTE12
- 4mob – hTE12 + ADP
- 3rd7 – TE – Mycobacterium avium
- 3u0a – TEII – Mycobacterium marinum
- 1tbu – TE N terminal (peroximal) – yeast
- 4qfw – YpTE II – Yersinia pestis
- 4r4u – YpTE II + CoA
Acyl protein thioesterase
- 1fj2 – EcTEI
Acyl-ACP thioesterase
- 2ess – TE – Bacterioides thetaiotaomicron
- 4gak – TE – Spirosoma linguale
- 4gwh – YpTE
ACP-polyene thioesterase
- 4i4j – TE – Streptomyces globisporus
Fluoroacetyl-CoA thioesterase
- 3kuv, 3kuw, 3kvi – ScTE (mutant) + acetate derivative – Streptomyces cattleya
- 3kv7, 3kv8, 3p2r, 3p2s – ScTE + acetate derivative
- 3kvu – ScTE + acetyl-CoA
- 3kvz, 3kw1 – ScTE + FAcOPan
- 3kx7, 3kx8, 3p2q – ScTE
- 3p3f – ScTE (mutant)
- 3p3i - ScTE (mutant) + acetate derivative + CoA
Dihydroxynaphthoyl-CoA thioesterase
- 4k00 – TE – Synechocystis
- 4k02 – AtTE – Arabidopsis thaliana
RedJ thioesterase
- 3qmv, 3qmw – TE – Streptomyces coelicolor
Orf6 thioesterase
- 4i45 – TE – Photobacterium profundum
thioesterase
- 2av9, 2o5u, 2o6b, 2o6t, 2o6u, 3qy3 – TE – Pseudomonas aeruginosa
Ubiquitin thioesterase
Ubiquitin thioesterase 2
- 2zfy – hUSP – human
- 2hd5, 3nhe, 3v6c, 3v6e – hUSP + Ub
- 1tff – hUSP (mutant)
- 2ibi – hUSP (mutant) + Ub
Ubiquitin thioesterase 3
- 2qiy – yUSP + USP-associated protein – yeast
Ubiquitin thioesterase 4
- 2y6e – hUSP catalytic domain
- 3jyu – mUSP N terminal domain - mouse
Ubiquitin thioesterase 5
- 2dag – hUSP UBA domain 1 - NMR
- 2dak – hUSP UBA domain 2 - NMR
- 2g43 – hUSP zinc finger USP domain
- 2g45 – hUSP zinc finger USP domain + Ub
- 3ihp – hUSP + Ub
Ubiquitin thioesterase 7
- 2f1z – hUSP
- 1nb8, 4m5w, 4m5x – hUSP catalytic domain
- 2kvr – hUSP UBL domain - NMR
- 4pyz – hUSP UBL domains 1+2
- 1yze, 2f1w – hUSP N terminal domain
- 2ylm – hUSP C terminal domain
- 2f1x, 2f1y, 2foj, 2foo, 2fop – hUSP N terminal domain/peptide
- 4zv3 – mUSP N terminal domain
Ubiquitin thioesterase 7 complexes
- 1nbf – hUSP catalytic domain + Ub aldehyde
- 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
- 4yoc – hUSP residues 560-1102 + DNA methyl transferase
Ubiquitin thioesterase 8
- 1whb – hUSP rhodanase domain - NMR
- 2a9u – hUSP N terminal domain
- 2gfo – hUSP catalytic domain
Ubiquitin thioesterase 8 complexes
- 2gwf – hUSP rhodanase domain + ring finger protein 41 USP8 interaction domain
- 3mhh, 3m99, 4fip, 4fjc, 4f5k, 4fk5 – yUSP + SUS1 + SGF11 +SGF73
- 3mhs – yUSP + SUS1 + SGF11 +SGF73 + Ub
- 3n3k – hUSP catalytic domain + Ub
Ubiquitin thioesterase 11
- 4mel – hUSP DUSP+UBL domains
- 4mem – rUSP DUSP+UBL domains - rat
Ubiquitin thioesterase 13
- 2l80 – hUSP zinc finger domain - NMR
- 2lbc – hUSP UBA domain - NMR
Ubiquitin thioesterase 14
- 1wgg – mUSP N terminal domain - NMR
- 2ayn – hUSP
- 2ayo – hUSP + Ub aldehyde
- 1wiv – AtUSP UBA domain - NMR
Ubiquitin thioesterase 15
- 3lmn – hUSP DUSP domain
- 3ppa, 3pv1, 3t9l, 4a3o, 4a3p – hUSP DUSP+UBL domains
- 1w6v – hUSP DUSP domain - NMR
Ubiquitin thioesterase 16
- 2i50 – hUSP zinc finger domain - NMR
Ubiquitin thioesterase 21
- 3i3t, 2y5b – hUSP + Ub
- 3mtn – hUSP + Ub inhibitor
Ubiquitin thioesterase 25
- 1vdl – mUSP catalytic domain
Ubiquitin thioesterase 28
- 2lva – hUSP N terminal - NMR
Ubiquitin thioesterase 33
- 2uzg – hUSP zinc finger domain - NMR
Ubiquitin thioesterase 37
- 3ihr – hUSP (mutant)
- 3a7s – hUSP catalytic domain (mutant)
- 3u12 – hUSP pleckstrin domain
Ubiquitin thioesterase 38
- 4rxx – hUSP N terminal
Ubiquitin thioesterase Cyld
- 2vhf – hUSP USP domain
Ubiquitin thioesterase L1
- 2etl – hUSP-L1
- 3irt, 4jkj – hUSP (mutant)
- 2len – hUSP (mutant) - NMR
- 3ifw, 3kvf, 3kw5 – hUSP (mutant) + Ub
- 4dm9 – hUSP + peptide inhibitor
Ubiquitin thioesterase L3
- 1uch – hUSP-L3
- 1xd3 – hUSP-L3 + UBC
- 2we6 – PfUSP-L3 – Plasmodium falciparum
- 2wdt – PfUSP-L3 + Ub
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
Ubiquitin thioesterase ZranB1
- 3zrh – hUSP
- 4s1z – bUSP zinc finger + Ub
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
Ubiquitin thioesterase
- 3znh – USP OTU domain + Ub – Crimean-Congo hemorrhagic fever virus
Pseudomonas aeruginosa TE
- 2av9, 2o5u, 2o6b, 2o6t, 2o6u, 3qy3 – PaTE – Pseudomonas aeruginosa
- 4qd7 – PaTE hotdog domain
- 4qda, 4qdb – PaTE hotdog domain (mutant)
- 4qd8, 4dq9 – PaTE hotdog domain + acyl-CoA derivatives

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
↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[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] 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

[7] 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

[8] 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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@@ Line 20: / Line 20: @@
 * USP33 regulates centrosome duplication.<br />
 * USP37 deubiquitinates cyclin A.<br />
+== Disease ==
+Mutations in palmiotoyl protein TE cause neuronal ceroid lipocfuscinosis<ref>PMID:7637805</ref><ref>PMID:11506414</ref>.
 == Structural highlights ==

Thioesterase: Difference between revisions

Revision as of 11:50, 11 September 2016

Contents

Function

Disease

Structural highlights

3D structures of thioesterase3D structures of thioesterase

ReferencesReferences

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Thioesterase: Difference between revisions

Revision as of 11:50, 11 September 2016

Function

Disease

Structural highlights

3D structures of thioesterase3D structures of thioesterase

ReferencesReferences

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