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| {{STRUCTURE_2iik| PDB=2iik | SIZE=400| SCENE=Thiolase/Thiolase/2 |right|CAPTION=Human 3-ketoacyl-CoA thiolase dimer, [[2iik]] }}
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| | <StructureSection load='4cij' size='350' side='right' caption='Human 3-ketoacyl-CoA complex with CoA (PDB code [[4cij]]).' scene=''> |
| == Function == | | == Function == |
| Two different classes of '''thiolases''' are found.<br /> | | Two different classes of '''thiolases''' are found.<br /> |
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| == Structural highlights == | | == Structural highlights == |
| The active site of 3-ketoacyl-CoA thiolase contains CoA<ref>PMID:25478839</ref>. | | The active site of 3-ketoacyl-CoA thiolase contains CoA<ref>PMID:25478839</ref>. |
| | </StructureSection> |
| == 3D Structures of Thiolase == | | == 3D Structures of Thiolase == |
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Revision as of 09:26, 12 September 2016
| Function
Two different classes of thiolases are found.
- Degrative thiolase like 3-ketoacyl-CoA thiolase (KCT) is involved in fatty acid β oxidation[1].
- Biosynthetic thiolases like acetoacetyl-CoA thiolase (ACT) are involved in the thiolysis of acetoacetyl-CoA[2].
For Bacterial thiolase see Bacterial thiolase
Structural highlights
The active site of 3-ketoacyl-CoA thiolase contains CoA[3].
- ↑ 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, 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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3D Structures of Thiolase
Updated on 12-September-2016
{"openlevels":0}
- 3-ketoacyl-CoA thiolase
- Bacterial thiolase, 2c7y, 2c7z – KCT peroxisomal residues 36-462 – Arabidopsis thaliana
- 2wua - KCT peroxisomal residues 17-449 (mutant) – sunflower
- 2iik – hKCT peroxisomal - human
- 4c2k – hKCT mitochondrial
- 4c2j – hKCT mitochondrial + CoA
- 3goa – KCT – Salmonella typhimurium
- 1afw, 1pxt – yKCT peroxisomal - yeast
- 3w15 - yKCT peroxisomal residues 27-396 + peroxiomal membrane protein PEX21 + peroxisomal targeting signal receptor
- 2d3t – PfKCT + fatty oxidation complex β subunit – Pseudomonas fragi
- 1wdk, 1wdl, 1wdm - PfKCT + fatty oxidation complex α subunit
- Acetoacetyl-CoA thiolase
- 1m4s, 1m4t, 1dlu, 1qfl - ZrACT – Zoogloea ramigera
- 1dm3, 1dlv – ZrACT + CoA
- 2wku, 2wl6, 1m1t, 1m3k - ZrACT (mutant)
- 2wkt, 2wkv, 2wl4, 2wl5, 2vtz, 2vu0, 1m3z – ZrACT (mutant) + CoA
- 1m1o - ZrACT (mutant) + acetoacetyl-CoA
- 2vu0, 1nl7 - ZrACT + CoA
- 2vu1, 2vu2, 1ou6 - ZrACT + pantheteine-11-pivalate
- 2ib7, 2ib8, 2ib9, 2ibu, 2ibw, 2iby, 2f2s – hACT mitochondrial
- 1wl5 - hACT cytosolic
- 1wl4 – hACT cytosolic + CoA
- 4dd5, 4e1l – ACT – Clostridium difficile
References
