Thioesterase
From Proteopedia
(Difference between revisions)
| Line 66: | Line 66: | ||
**[[2v1o]] – mTE7 hotdog domain – mouse<br /> | **[[2v1o]] – mTE7 hotdog domain – mouse<br /> | ||
**[[2q2b]] – mTE7 C terminal<br /> | **[[2q2b]] – mTE7 C terminal<br /> | ||
| + | **[[2pzh]] - TE - ''Helicobacter pylori''<br /> | ||
**[[3hlk]] – hTE2<br /> | **[[3hlk]] – hTE2<br /> | ||
**[[3k2i]] – hTE4<br /> | **[[3k2i]] – hTE4<br /> | ||
| Line 169: | Line 170: | ||
*Ubiquitin thioesterase 8 | *Ubiquitin thioesterase 8 | ||
| - | **[[1whb]] – hUSP rhodanase domain | + | **[[1whb]] – hUSP rhodanase domain - NMR<br /> |
**[[2a9u]] – hUSP N terminal domain <br /> | **[[2a9u]] – hUSP N terminal domain <br /> | ||
**[[2gfo]] – hUSP catalytic domain <br /> | **[[2gfo]] – hUSP catalytic domain <br /> | ||
| Line 293: | Line 294: | ||
*Pseudomonas aeruginosa TE | *Pseudomonas aeruginosa TE | ||
| - | **[[2av9]], [[2o5u]], [[2o6b]], [[2o6t]], [[2o6u]], [[3qy3]] – PaTE – Pseudomonas aeruginosa | + | **[[2av9]], [[2o5u]], [[2o6b]], [[2o6t]], [[2o6u]], [[3qy3]] – PaTE – ''Pseudomonas aeruginosa''<br /> |
**[[4qd7]] – PaTE hotdog domain<br /> | **[[4qd7]] – PaTE hotdog domain<br /> | ||
**[[4qda]], [[4qdb]] – PaTE hotdog domain (mutant)<br /> | **[[4qda]], [[4qdb]] – PaTE hotdog domain (mutant)<br /> | ||
Revision as of 07:46, 29 February 2016
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. For details see Palmitoyl protein thioesterase.
- 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. 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.
- 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 29-February-2016
