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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:
Succinyl CoA:3-oxoacid CoA transferase (EC 18.104.22.168) (SCOT), which is
responsible for the formation of acetoacetyl CoA by transfer of a CoA
moiety from succinyl-CoA to a 3-oxoacid, usually acetoacetate. In higher
eukaryotes it is a mitochondrial enzyme which plays a crucial role in
ketone body metabolism. It has also been found in bacteria.
Bacterial 3-oxoadipate CoA-transferase (EC 22.214.171.124) which carries out the
penultimate step in the conversion of benzoate and 4-hydroxybenzoate to
tricarboxylic acid cycle intermediates in bacteria utilizing the β-
Clostridial butyrate-acetoacetate CoA-transferase (EC 126.96.36.199), which acts
mainly to detoxify the medium by removing the acetate and butyrate excreted
earlier in the fermentation.
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 .
November 1997 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
Parales R.E., Harwood C.S.
Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida.
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