Thiolase
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | <StructureSection load='4c2j' size='350' side='right' caption='Human 3-ketoacyl-CoA complex with CoA and ethylene glycol(PDB code [[4c2j]]) | + | <StructureSection load='4c2j' size='350' side='right' caption='Human 3-ketoacyl-CoA complex with CoA and ethylene glycol (PDB code [[4c2j]])' scene='44/447919/Cv/7'> |
== Function == | == Function == | ||
Two different classes of '''thiolases''' are found.<br /> | Two different classes of '''thiolases''' are found.<br /> | ||
| - | *'''Degrative thiolase''' like '''3-ketoacyl-CoA thiolase''' (KCT) is involved in fatty acid | + | *'''Degrative thiolase''' like '''3-ketoacyl-CoA thiolase''' (KCT) is involved in fatty acid [[beta oxidation]]<ref>PMID:16630629</ref>.<br /> |
*'''Biosynthetic thiolases''' like '''acetoacetyl-CoA thiolase''' (ACT) or '''acetyl-CoA acetyltransferase''' are involved in the thiolysis of acetoacetyl-CoA<ref>PMID:21908473</ref>. | *'''Biosynthetic thiolases''' like '''acetoacetyl-CoA thiolase''' (ACT) or '''acetyl-CoA acetyltransferase''' are involved in the thiolysis of acetoacetyl-CoA<ref>PMID:21908473</ref>. | ||
For bacterial thiolase see [[Bacterial thiolase]] | For bacterial thiolase see [[Bacterial thiolase]] | ||
| - | For zebrafish thiolase see [[SCP2-thiolase]] | + | *'''SCP2-thiolase''' converts in the bile acid synthesis pathway 24-keto-THC-CoA into choloyl-CoA and propionyl-CoA<ref>PMID:30573650</ref>. For zebrafish thiolase see [[SCP2-thiolase]]. ''' SCP''' is Sterol Carrier Protein. |
| + | *'''U34-tRNA-thiolase''' thiolates uridine 34 in tRNA anticodon loop which guarantees the fidelity of protein translation in archaea<ref>PMID:37005440</ref>. | ||
| + | |||
| + | See also [[Mevalonate pathway]] | ||
== Structural highlights == | == Structural highlights == | ||
Current revision
| |||||||||||
References
- ↑ Sundaramoorthy R, Micossi E, Alphey MS, Germain V, Bryce JH, Smith SM, Leonard GA, Hunter WN. The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation. J Mol Biol. 2006 Jun 2;359(2):347-57. Epub 2006 Mar 29. PMID:16630629 doi:http://dx.doi.org/10.1016/j.jmb.2006.03.032
- ↑ Soto G, Stritzler M, Lisi C, Alleva K, Pagano ME, Ardila F, Mozzicafreddo M, Cuccioloni M, Angeletti M, Ayub ND. Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation. J Exp Bot. 2011 Nov;62(15):5699-711. doi: 10.1093/jxb/err287. Epub 2011 Sep 9. PMID:21908473 doi:http://dx.doi.org/10.1093/jxb/err287
- ↑ Kiema TR, Thapa CJ, Laitaoja M, Schmitz W, Maksimainen MM, Fukao T, Rouvinen J, Janis J, Wierenga RK. The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry. Biochem J. 2018 Dec 20. pii: BCJ20180788. doi: 10.1042/BCJ20180788. PMID:30573650 doi:http://dx.doi.org/10.1042/BCJ20180788
- ↑ Bimai O, Legrand P, Ravanat JL, Touati N, Zhou J, He N, Lénon M, Barras F, Fontecave M, Golinelli-Pimpaneau B. The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis. Sci Rep. 2023 Apr 1;13(1):5351. PMID:37005440 doi:10.1038/s41598-023-32423-9
- ↑ Kiema TR, Harijan RK, Strozyk M, Fukao T, Alexson SE, Wierenga RK. The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3212-25. doi:, 10.1107/S1399004714023827. Epub 2014 Nov 22. PMID:25478839 doi:http://dx.doi.org/10.1107/S1399004714023827
