Biology:3-oxoacid CoA-transferase

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Short description: Enzyme family
3-oxoacid CoA-transferase (SCOT)
Pig succinyl-CoA 3-oxoacid transferase (SCOT) PDB 3K6M.png
Pig succinyl-CoA 3-oxoacid transferase PDB: 3K6M
Identifiers
EC number2.8.3.5
CAS number9027-43-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a 3-oxoacid CoA-transferase (EC 2.8.3.5) is an enzyme that catalyzes the chemical reaction

succinyl-CoA + a 3-oxo acid [math]\displaystyle{ \rightleftharpoons }[/math] succinate + a 3-oxoacyl-CoA

Thus, the two substrates of this enzyme are succinyl-CoA and 3-oxo acid, whereas its two products are succinate and 3-oxoacyl-CoA.

This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:3-oxo-acid CoA-transferase. Other names in common use include succinyl-CoA-3-ketoacid-CoA transferase, 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A transferase, 3-oxo-CoA transferase, 3-oxoacid CoA dehydrogenase, acetoacetate succinyl-CoA transferase, acetoacetyl coenzyme A-succinic thiophorase, succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. This enzyme participates in 3 metabolic pathways: synthesis and degradation of ketone bodies,[1] valine, leucine and isoleucine degradation, and butanoate metabolism.

This protein may use the morpheein model of allosteric regulation.[2]

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1M3E, 1O9L, 1OOY, 1OOZ, 1OPE, 2NRB, and 2NRC.

References

  1. Blanco, Antonio; Blanco, Gustavo (2017), "Chapter 15 - Lipid Metabolism" (in en), Medical Biochemistry (Academic Press): pp. 325–365, doi:10.1016/b978-0-12-803550-4.00015-x, ISBN 978-0-12-803550-4, https://www.sciencedirect.com/science/article/pii/B978012803550400015X, retrieved 2023-06-08 
  2. T. Selwood; E. K. Jaffe (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMID 22182754.