Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence.
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.
Vettakkorumakankav
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Department of Biological Sciences, University of Calgary, Alta., Canada.
Danson
M J
MJ
Hough
D W
DW
Stevenson
K J
KJ
Davison
M
M
Young
J
J
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
D000596:Amino Acids; D001152:Arsenicals; D004112:Dimercaprol; D005182:Flavin-Adenine Dinucleotide; C007409:dihydrolipoamide; D012965:Sodium Chloride; D008063:Thioctic Acid; D008058:Dihydrolipoamide Dehydrogenase