Thiolase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:15, 18 August 2024) (edit) (undo)
 
(30 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='4c2j' size='450' side='right' caption='Human 3-ketoacyl-CoA complex with CoA and ethylene glycol(PDB code [[4c2j]]).' scene='44/447919/Cv/1'>
+
<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 β oxidation<ref>PMID:16630629</ref>.<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) 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]]
 +
 
 +
*'''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 ==
-
The <scene name='44/447919/Cv/4'>active site of 3-ketoacyl-CoA thiolase contains CoA</scene><ref>PMID:25478839</ref>. Water molecules shown as red spheres.
+
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.
-
</StructureSection>
+
== 3D Structures of Thiolase ==
== 3D Structures of Thiolase ==
 +
[[Thiolase 3D structures]]
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
</StructureSection>
-
{{#tree:id=OrganizedByTopic|openlevels=0|
+
-
 
+
-
*3-ketoacyl-CoA thiolase
+
-
 
+
-
**[[2wu9]], [[2c7y]], [[2c7z]] – KCT peroxisomal residues 36-462 – ''Arabidopsis thaliana''<br />
+
-
**[[2wua]] - KCT peroxisomal residues 17-449 (mutant) – sunflower<br />
+
-
**[[2iik]] – hKCT peroxisomal – human<br />
+
-
**[[4c2k]] – hKCT mitochondrial <br />
+
-
**[[4c2j]] – hKCT mitochondrial + CoA<br />
+
-
**[[3goa]] – KCT – ''Salmonella typhimurium''<br />
+
-
**[[5lp7]] – KCT – ''Bacillus subtilis'' <br />
+
-
**[[1afw]], [[1pxt]] – yKCT peroxisomal – yeast<br />
+
-
**[[5cbq]] – MsKCT – ''Mycobacterium smegmatis'' <br />
+
-
**[[4w61]] – ReKCT – ''Ralstonia eutropha''<br />
+
-
**[[4ubw]] – MtKCT – ''Mycobacterium tuberculosis'' <br />
+
-
 
+
-
*3-ketoacyl-CoA thiolase complex
+
-
 
+
-
**[[3w15]] - yKCT peroxisomal residues 27-396 + peroxiomal membrane protein PEX21 + peroxisomal targeting signal receptor<br />
+
-
**[[2d3t]] – PfKCT + fatty oxidation complex β subunit – ''Pseudomonas fragi''<br />
+
-
**[[1wdk]], [[1wdl]], [[1wdm]] - PfKCT + fatty oxidation complex α subunit<br />
+
-
**[[5bz4]] – MsKCT + CoA <br />
+
-
**[[4ubt]] – MtKCT (mutant) + CoA + steroid <br />
+
-
**[[4ubu]] – MtKCT (mutant) + CoA <br />
+
-
**[[4ubv]] – MtKCT + CoA + acetyl CoA <br />
+
-
 
+
-
*Acetoacetyl-CoA thiolase
+
-
 
+
-
**[[1m4s]], [[1m4t]], [[1dlu]], [[1qfl]] - ZrACT – ''Zoogloea ramigera''<br />
+
-
**[[2wku]], [[ 2wl6]], [[1m1t]], [[1m3k]] - ZrACT (mutant) <br />
+
-
**[[2ib7]], [[ 2ib8]], [[2ib9]], [[2ibu]], [[2ibw]], [[2iby]], [[2f2s]] – hACT mitochondrial<br />
+
-
**[[1wl5]] - hACT cytosolic<br />
+
-
**[[4dd5]], [[4e1l]] – ACT – ''Clostridium difficile''<br />
+
-
**[[4xl2]], [[4xl3]], [[4n44]], [[4n45]] – CaACT – ''Clostridium acetobutylicum''<br />
+
-
**[[4wyr]] – CaACT (mutant) <br />
+
-
**[[5f0v]], [[ [[5f38]], [[4wys]] – ACT – ''Escherichia coli'' <br />
+
-
**[[4o9a]], [[4o99]], [[4o9c]], [[4nzs]] – ReACT <br />
+
-
 
+
-
*Acetoacetyl-CoA thiolase complex
+
-
 
+
-
**[[1dm3]], [[1dlv – ZrACT + CoA<br />
+
-
**[[2wkt]], [[2wkv]], [[2wl4]], [[2wl5]], [[2vtz]], [[1m3z]] – ZrACT (mutant) + CoA<br />
+
-
**[[1m1o]] - ZrACT (mutant) + acetoacetyl-CoA<br />
+
-
**[[2vu0]], [[1nl7]] - ZrACT + CoA<br />
+
-
**[[2vu1]], [[2vu2]], [[1ou6]] - ZrACT + pantheteine-11-pivalate<br />
+
-
**]]1wl4]] – hACT cytosolic + CoA <br />
+
-
**[[4xl4]] – CaACT + CoA <br />
+
-
}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

References

  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:http://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:http://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:http://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:http://dx.doi.org/10.1107/S1399004714023827

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Thiolase"
Personal tools