title: Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence.
abstract: Dihydrolipoamide dehydrogenase, a flavin disulfide reductase, has been purified and characterized from Haloferax volcanii. The enzyme is a dimer of relative mass 128,000, with an optimal activity at pH 9.0 in 1 M NaCl. Following reduction with its substrate, dihydrolipoamide, the enzyme is inactivated through covalent bond formation with the trivalent arsenical p-aminophenyl arsenoxide. The amino acid composition and the amino acid sequence of the first 49 residues of the N-terminus have been determined.
authors.affiliation: Department of Biological Sciences, University of Calgary, Alta., Canada.
authors.forename: N
authors.initials: N
authors.lastname: Vettakkorumakankav
authors.forename: M J
authors.initials: MJ
authors.lastname: Danson
authors.forename: D W
authors.initials: DW
authors.lastname: Hough
authors.forename: K J
authors.initials: KJ
authors.lastname: Stevenson
authors.forename: M
authors.initials: M
authors.lastname: Davison
authors.forename: J
authors.initials: J
authors.lastname: Young
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001105:Archaea / Q000201:enzymology*; D001152:Arsenicals; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D004112:Dimercaprol / Q000494:pharmacology; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D012965:Sodium Chloride / Q000494:pharmacology; D008063:Thioctic Acid / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D001152:Arsenicals; D004112:Dimercaprol; D005182:Flavin-Adenine Dinucleotide; C007409:dihydrolipoamide; D012965:Sodium Chloride; D008063:Thioctic Acid; D008058:Dihydrolipoamide Dehydrogenase