A lipoamide dehydrogenase from Neisseria meningitidis has a lipoyl domain
- 1 April 1995
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 21 (4) , 303-306
- https://doi.org/10.1002/prot.340210404
Abstract
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.Keywords
This publication has 18 references indexed in Scilit:
- Three-dimensional Structure of Lipoamide Dehydrogenase from Pseudomonas fluorescens at 2·8 Å Resolution: Analysis of Redox and Thermostability PropertiesJournal of Molecular Biology, 1993
- Refined Crystal Structure of the Catalytic Domain of Dihydrolipoyl Transacetylase (E2p) from Azotobacter vinelandii at 2·6 Å ResolutionJournal of Molecular Biology, 1993
- Three-dimensional Structure of the Lipoyl domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme ComplexJournal of Molecular Biology, 1993
- Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coliBiochemistry, 1992
- Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolutionJournal of Molecular Biology, 1991
- Dihydrolipoamide dehydrogenase: Functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductasesArchives of Biochemistry and Biophysics, 1989
- Dihydrolipoamide dehydrogenase from halophilic archaebacteria: purification and properties of the enzyme from Halobacterium halobiumBiochemistry, 1986
- Galactose- and maltose-stimulated lipoamide dehydrogenase activities related to the binding-protein-dependent transport of galactose and maltose in toluenized cells of Escherichia coliEuropean Journal of Biochemistry, 1986
- Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12European Journal of Biochemistry, 1983
- IDENTIFICATION OF ANTIGEN 19/27 AS DIHYDROLIPOYL DEHYDROGENASE AND ITS PROBABLE INVOLVEMENT IN UBIQUINONE-MEDIATED NADH-DEPENDENT TRANSPORT PHENOMENA IN MEMBRANE VESICLES OFESCHERICHIA COLIFEMS Microbiology Letters, 1980