Thioesterase

Revision as of 09:12, 31 December 2014 by Michal Harel (Talk | contribs)

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.
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.