A lipoamide dehydrogenase from Neisseria meningitidis has a lipoyl domain.
A protein of molecular weight of 64 kDa (p64k) found in the outer membrane of Neisseria meningitidis shows a high degree of homology with both the lipoyl domain of the acetyltransferase and the entire sequence of the lipoamide dehydrogenase, the E2 and E3 components of the dehydrogenase multienzyme complexes, respectively. The alignment of the p64k with lipoyl domains and lipoamide dehydrogenases from different species is presented. The possible implications of this protein in binding protein-dependent transport are discussed. This is the first lipoamide dehydrogenase reported to have a lipoyl domain.
Bringas
R
R
Center for Genetic Engineering and Biotechnology, Havana, Cuba.
Fernandez
J
J
D000595:Amino Acid Sequence; D015139:Blotting, Southern; D015153:Blotting, Western; D002462:Cell Membrane / Q000737:chemistry / Q000201:enzymology; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry* / Q000201:enzymology*; D011485:Protein Binding; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D008058:Dihydrolipoamide Dehydrogenase