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    Biochem Cell Biol. 1992 Jan;70(1):70-5.

    Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence.

    Vettakkorumakankav N, Danson MJ, Hough DW, Stevenson KJ, Davison M, Young J.

    Department of Biological Sciences, University of Calgary, Alta., Canada.

    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.

    PMID: 1581034 [PubMed - indexed for MEDLINE]

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