|PROSITE documentation PDOC00980|
Coenzyme A (CoA) transferases are enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. They belong to an evolutionary conserved [1,2] family of proteins that consist of:
The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.
We developed two signature patterns for these enzymes. The first corresponds to a region in the N-terminal of the A subunit that may be implicated in the binding of CoA to the enzyme. The second corresponds to a region in the N-terminal of the B subunit and contains a glutamate that is involved in the catalytic mechanism .Last update:
November 1997 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Parales R.E. Harwood C.S.|
|Title||Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.|
|Source||J. Bacteriol. 174:4657-4666(1992).|
|2||Authors||Corthesy-Theulaz I.E. Bergonzelli G.E. Henry H. Bachmann D. Schorderet D.F. Blum A.L. Ornston L.N.|
|Source||J. Biol. Chem. 272:25659-25667(1997).|
|3||Authors||Rochet J.C. Bridger W.A.|
|Title||Identification of glutamate 344 as the catalytic residue in the active site of pig heart CoA transferase.|
|Source||Protein Sci. 3:975-981(1994).|