Related Experiment Videos
Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and
N Vettakkorumakankav1, M J Danson, D W Hough
1Department of Biological Sciences, University of Calgary, Alta., Canada.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|January 1, 1992
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.