Cryptic proteolytic activity of dihydrolipoamide dehydrogenase

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Dihydrolipoamide dehydrogenase from halophilic archaebacteria.

Dihydrolipoamide dehydrogenase has been discovered in the halophilic archaebacteria for the first time. The enzyme from both classical and alkaliphilic halobacteria has been investigated. (1) The enzyme specifically catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+. Enzymic activity was optimal at 2 M-NaCl and was remarkably resistant to thermal denaturation. (2) The relative m...

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Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine.

Dihydrolipoamide dehydrogenase (E3) belongs to the pyridine nucleotide-disulfide oxidoreductase family including glutathione reductase and thioredoxin reductase. It catalyzes the reoxidation of dihydrolipoyl moiety of the acyltransferase components of three alpha-keto acid dehydrogenase complexes and of the hydrogen-carrier protein of the glycine cleavage system. Isoleucine-51 of human E3, loca...

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Induction of dihydrolipoamide dehydrogenase in 3T3-L1 cells during differentiation.

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2007

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.0610618104