Thioesterase
From Proteopedia
(Difference between revisions)
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**[[4k00]] – TE – ''Synechocystis''<br /> | **[[4k00]] – TE – ''Synechocystis''<br /> | ||
**[[4k02]] – TE – ''Arabidopsis thaliana''<br /> | **[[4k02]] – TE – ''Arabidopsis thaliana''<br /> | ||
| + | |||
| + | *RedJ thioesterase | ||
| + | |||
| + | **[[3qmv]], [[3qmw]] – TE –'' Streptomyces coelicolor'' | ||
| + | |||
| + | *Orf6 thioesterase | ||
| + | |||
| + | **[[4i45]] – TE – ''Photobacterium profundum''<br /> | ||
| + | |||
| + | *thioesterase | ||
| + | |||
| + | **[[2av9]], [[2o5u]], [[2o6b]], [[2o6t]], [[2o6u]], [[3qy3]] – TE – ''Pseudomonas aeruginosa'' | ||
*Ubiquitin thioesterase | *Ubiquitin thioesterase | ||
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**[[3znh]] – USP OTU domain + Ub – Crimean-Congo hemorrhagic fever virus<BR /> | **[[3znh]] – USP OTU domain + Ub – Crimean-Congo hemorrhagic fever virus<BR /> | ||
| - | *RedJ thioesterase | ||
| - | |||
| - | **[[3qmv]], [[3qmw]] – TE –'' Streptomyces coelicolor'' | ||
| - | |||
| - | *Orf6 thioesterase | ||
| - | |||
| - | **[[4i45]] – TE – ''Photobacterium profundum''<br /> | ||
| - | |||
| - | *thioesterase | ||
| - | |||
| - | **[[2av9]], [[2o5u]], [[2o6b]], [[2o6t]], [[2o6u]], [[3qy3]] – TE – ''Pseudomonas aeruginosa'' | ||
}} | }} | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:25, 11 December 2014
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 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 (UB). The USPs are involved in the processing of poly-UB precursors and of ubiquinated proteins. 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.
3D structures of thioesterase
Updated on 11-December-2014
