|PROSITE documentation PDOC00168|
The 2-oxo acid dehydrogenase multienzyme complexes [1,2] from bacterial and eukaryotic sources catalyze the oxidative decarboxylation of 2-oxo acids to the corresponding acyl-CoA. The three members of this family of multienzyme complexes are:
These three complexes share a common architecture: they are composed of multiple copies of three component enzymes - E1, E2 and E3. E1 is a thiamine pyrophosphate-dependent 2-oxo acid dehydrogenase, E2 a dihydrolipamide acyltransferase, and E3 an FAD-containing dihydrolipamide dehydrogenase.
E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via a amide linkage to a lysine group. The E2 components of OGCD and BCOACD bind a single lipoyl group, while those of PDC bind either one (in yeast and in Bacillus), two (in mammals), or three (in Azotobacter and in Escherichia coli) lipoyl groups .
In addition to the E2 components of the three enzymatic complexes described above, a lipoic acid cofactor is also found in the following proteins:
We developed a signature pattern which allows the detection of the lipoyl-binding site.Note:
The domain around the lipoyl-binding lysine residue is evolutionary related to that around the biotin-binding lysine residue of biotin requiring enzymes (see <PDOC00167>).Last update:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|Title||The 2-oxo acid dehydrogenase complexes: recent advances.|
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|Source||Trends Biochem. Sci. 11:293-296(1986).|
|3||Authors||Russel G.C. Guest J.R.|
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|4||Authors||Fujiwara K. Okamura-Ikeda K. Motokawa Y.|
|Title||Chicken liver H-protein, a component of the glycine cleavage system. Amino acid sequence and identification of the N epsilon-lipoyllysine residue.|
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|Title||Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism.|
|Source||J. Bacteriol. 173:4056-4071(1991).|