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Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases

Delaney, Robert ; Burns, Gayle ; Sokatch, John R

FEBS Letters, 1984, Vol.168(2), pp.265-270 [Periódico revisado por pares]

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  • Título:
    Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases
  • Autor: Delaney, Robert ; Burns, Gayle ; Sokatch, John R
  • Assuntos: Lipoamide Dehydrogenase ; Branched-Chain Keto Acid Dehydrogenase ; Pseudomonas Putida ; Biology ; Chemistry ; Anatomy & Physiology
  • É parte de: FEBS Letters, 1984, Vol.168(2), pp.265-270
  • Descrição: Pseudomonas putida produces two lipoamide dehydrogenases, LPD-glc and LPD-val. LPD-val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase and LPD-glc fulfills all other requirements for lipoamide dehydrogenase. Both proteins are dimers with one FAD per subunit. LPD-glc has an absorption maximum at 455 nm, but LPD-val has a maximum at 460 nm. Comparison of amino acid compositions revealed that LPD-glc was more closely related to Escherichia coli and pig heart lipoamide dehydrogenase than to LPD-val. LPD-val did not appear to be closely related to any of the proteins compared with the possible exception of mercuric reductase.
  • Idioma: Inglês

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