Thiolase: Difference between revisions

Latest revision as of 10:15, 18 August 2024

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Human 3-ketoacyl-CoA complex with CoA and ethylene glycol (PDB code 4c2j)

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Function

Two different classes of thiolases are found.

Degrative thiolase like 3-ketoacyl-CoA thiolase (KCT) is involved in fatty acid beta oxidation^[1].
Biosynthetic thiolases like acetoacetyl-CoA thiolase (ACT) or acetyl-CoA acetyltransferase are involved in the thiolysis of acetoacetyl-CoA^[2].

For bacterial thiolase see Bacterial thiolase

SCP2-thiolase converts in the bile acid synthesis pathway 24-keto-THC-CoA into choloyl-CoA and propionyl-CoA^[3]. 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^[4].

Structural highlights

The active site of 3-ketoacyl-CoA thiolase contains CoA^[5]. Water molecules are shown as red spheres.

3D Structures of Thiolase

Thiolase 3D structures

↑ 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:https://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:https://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:https://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:https://dx.doi.org/10.1107/S1399004714023827

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] 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:https://dx.doi.org/10.1016/j.jmb.2006.03.032

[2] 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:https://dx.doi.org/10.1093/jxb/err287

[3] 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:https://dx.doi.org/10.1042/BCJ20180788

[4] 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

[5] 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:https://dx.doi.org/10.1107/S1399004714023827

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@@ Line 1: / Line 1: @@
-[[Image:2iik.png|left|200px|thumb|Crystal Structure of Thiolase, [[2iik]]]]
+<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'>
-{{STRUCTURE_2iik|  PDB=2iik  | SIZE=400| SCENE=Thiolase/Thiolase/2 |right|CAPTION=Human 3-ketoacyl-CoA thiolase dimer, [[2iik]] }}
+== Function ==
+Two different classes of '''thiolases''' are found.<br />
+*'''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>.
+For bacterial thiolase see [[Bacterial 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 ==
+The <scene name='44/447919/Cv/8'>active site of 3-ketoacyl-CoA thiolase contains CoA</scene><ref>PMID:25478839</ref>. Water molecules are shown as red spheres.
-'''Thiolase''' involves two different thiolases .  The 3-ketoacyl-CoA thiolase (KCT) is involved in fatty acid β oxidation. Acetoacetyl-CoA thiolase (ACT) is involved in the thiolysis of acetoacetyl-CoA.
-{{TOC limit|limit=2}}
-For Bacterial Thiolase see [[Bacterial thiolase]]
 == 3D Structures of Thiolase ==
+[[Thiolase 3D structures]]
+</StructureSection>
-===3-ketoacyl-CoA thiolase===
+== References ==
+<references/>
-[[2wu9]], [[2c7y]], [[2c7z]] – KCT peroxisomal residues 36-462 – ''Arabidopsis thaliana''<br />
-[[2wua]] - KCT peroxisomal residues 17-449 (mutant) – sunflower<br />
-[[2iik]] – hKCT peroximal - human<br />
-[[3goa]] – KCT – ''Salmonella typhimurium''<br />
-[[1afw]], [[1pxt]] – KCT peroxisomal - yeast<br />
-[[2d3t]] – PfKCT + fatty oxidation complex β subunit – ''Pseudomonas fragi''<br />
-[[1wdk]], [[1wdl]], [[1wdm]] - PfKCT + fatty oxidation complex α subunit
-===Acetoacetyl-CoA thiolase===
-[[1m4s]], [[1m4t]], [[1dlu]], [[1qfl]] - ZrACT – ''Zoogloea ramigera''<br />
-[[1dm3]], [[1dlv]] – ZrACT + CoA<br />
-[[2wku]], [[2wl6]], [[1m1t]], [[1m3k]] - ZrACT (mutant) <br />
-[[2wkt]], [[2wkv]], [[2wl4]], [[2wl5]], [[2vtz]], [[2vu0]], [[1m3z]] – ZrACT (mutant) + CoA<br />
-[[1m1o]] - ZrACT (mutant) + acetoacetyl-CoA<br />
-[[2vu0]], [[1nl7]] - ZrACT + CoA<br />
-[[2vu1]], [[2vu2]], [[1ou6]] - ZrACT + pantheteine-11-pivalate<br />
-[[2ib7]], [[2ib8]], [[2ib9]], [[2ibu]], [[2ibw]], [[2iby]], [[2f2s]] – hACT mitochondrial<br />
-[[1wl5]] - hACT cytosolic<br />
-[[1wl4]] – hACT cytosolic + CoA<br />
 [[Category:Topic Page]]

Thiolase: Difference between revisions

Latest revision as of 10:15, 18 August 2024

Function

Structural highlights

3D Structures of Thiolase

References

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