Thioesterase: Difference between revisions

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'''Thioesterase''' (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group.  TEs are substrate-specific.<br />
'''Thioesterase''' (TE) catalyzes the break of an ester bond to produce acid and alcohol at a thiol group.  TEs are substrate-specific.<br />
*  '''Palmitoyl protein TE''' removes fatty acids like palmitate from modified cysteine residues during lysosomal degradation<ref>PMID:10737604</ref.  For details see [[Palmitoyl protein thioesterase]].<br />
*  '''Palmitoyl protein TE''' removes fatty acids like palmitate from modified cysteine residues during lysosomal degradation<ref>PMID:10737604</ref>.  For details see [[Palmitoyl protein thioesterase]].<br />
*  '''4-hydroxybenzoyl-CoA TE''' converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA<ref>PMID:12732540</ref.<br />
*  '''4-hydroxybenzoyl-CoA TE''' converts 4-hydroxybenzoyl-CoA to 4-hydroxybenzoate and CoA<ref>PMID:12732540</ref>.<br />
*  '''Acyl-CoA TE''' hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism<ref>PMID:11755680</ref.  See also [[YbgC]].<br />
*  '''Acyl-CoA TE''' hydrolyzes acyl-CoA to the fatty acid and CoA and is involved in lipid metabolism<ref>PMID:11755680</ref>.  See also [[YbgC]].<br />
*  '''Fluoroacetyl-CoA TE''' from ''Streptomyces cattleya'' hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate.<br />
*  '''Fluoroacetyl-CoA TE''' from ''Streptomyces cattleya'' hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate.<br />
*  '''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.  
*  '''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.  

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Michal Harel, Alexander Berchansky, Joel L. Sussman