Thioesterase: Difference between revisions
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< | <StructureSection load='' size='350' side='right' caption='Human ubiquitin esterase 2 (deepskyblue) complex with ubiquitin (green) and zinc+2 ion (grey) (PDB code [[2hd5]]).' scene='48/489265/Cv/2'> | ||
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== Function == | |||
'''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 /> | |||
'''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 removes conjugated ubiquitin from proteins thus regulating protein level by preventing their degradation. | * '''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]] and [[Mitochondrial hotdog-fold thioesterase]].<br /> | |||
* '''Fluoroacetyl-CoA TE''' from ''Streptomyces cattleya'' hydrolyzes fluoroacetyl-CoA thus preventing it from being metabolized to the lethal 4-hydroxy-trans-aconitate<ref>PMID:20836570</ref>.<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. The USPs are involved in the processing of poly-UB precursors and of ubiquitinated proteins<ref>PMID:24190967</ref>. USP contains catalytic domain surrounded several domains: Ub-like (UBL); Ub-associated (UBA); zinc finger-Ub-specific protease domain (UBP or DUSP); TRAF homology domain. | |||
* '''USP-L1, USP25''' hydrolyze C-terminal adducts of UB.<br /> | |||
* '''USP-L3''' hydrolyzes C-terminal adducts of UB and NEDD8.<br /> | |||
* '''USP5''' cleaves multiubiquitin polymers.<br /> | |||
* '''USP6''' has ATP-independent isopeptidase activity.<br /> | |||
* '''USP7, USP4, USP13, USP15''' deubiquitinate several proteins.<br /> | |||
* '''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.<br /> | |||
* '''USP11, USP14''' are proteasome-associated.<br /> | |||
* '''USP12''' stabilizes T-cell complexes<ref>PMID:26811477</ref>.<br /> | |||
* '''USP16, USP21''' deubiquitinate histone H2A.<br /> | |||
* '''USP18''' is a down regulator of the type I interferon signaling pathway<ref>PMID:23700969</ref>.<br /> | |||
* '''USP28''' deubiquitinates proteins of the DNA damage pathway.<br /> | |||
* '''USP33''' regulates centrosome duplication.<br /> | |||
* '''USP37''' deubiquitinates cyclin A.<br /> | |||
* '''USP46''' deubiquitinates AMPA receptor<ref>PMID:26077708</ref>.<br /> | |||
== Disease == | |||
Mutations in palmiotoyl protein TE cause neuronal ceroid lipocfuscinosis<ref>PMID:7637805</ref><ref>PMID:11506414</ref>. | |||
== Structural highlights == | |||
<scene name='48/489265/Cv/7'>Human ubiquitin esterase 2 complex with ubiquitin and zinc+2 ion</scene>. Ubiquitin thioesterase 2 active site contains the <scene name='48/489265/Cv/8'>catalytic triad Cys-His-Asn and the oxyanion hole Asn</scene>. The metal-binding enzyme contains a <scene name='48/489265/Cv/9'>Zn+2 ion which coordinates to 4 Cys residues</scene>. The <scene name='48/489265/Cv/10'>ubiquitin coordinates to the thioesterase via residues in all thioesterase domains: finger, palm and thumb</scene><ref>PMID:16905103</ref>. | |||
==3D structures of thioesterase== | |||
[[Thioesterase 3D structures]] | |||
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[[ | |||
</StructureSection> | |||
[[ | == References == | ||
<references/> | |||
[[Category:Topic Page]] |