Template:STRUCTURE 1u8u

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 thioesterase3D structures of thioesterase

Updated on 11-December-2014

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Michal Harel, Alexander Berchansky, Joel L. Sussman