IntEnz

EC 2.8.3.8 - Acetate CoA-transferase

IntEnz Enzyme Nomenclature
EC 2.8.3.8

Names

Reaction

• 13381 [IUBMB]
  acetate

  acetate

  Name origin: UniProt - CHECKED (C)

  CHEBI:30089

  Formula: C2H3O2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  an acyl-CoA

  an acyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:58342

  Formula: C22H31N7O17P3SR
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  =

  a fatty acid

  a fatty acid

  Name origin: UniProt - CHECKED (C)

  CHEBI:28868

  Formula: CO2R
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  acetyl-CoA

  acetyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57288

  Formula: C23H34N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

Comments:

The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate—acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA.

Links to other databases

References

1. Vanderwinkel, E., Furmanski, P., Reeves, H.C. and Ajl, S.J.
   Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity.
   Biochem. Biophys. Res. Commun. 33: 902-908 (1968). [PMID: 4884054]
2. Rangarajan, E. S., Li, Y., Ajamian, E., Iannuzzi, P., Kernaghan, S. D., Fraser, M. E., Cygler, M., Matte, A.
   Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.
   J. Biol. Chem. 280: 42919-42928 (2005). [PMID: 16253988]

[EC 2.8.3.8 created 1972]