Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D008058:Dihydrolipoamide Dehydrogenase / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis*; D005980:Glutathione Reductase / Q000032:analysis; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology; D010088:Oxidoreductases / Q000032:analysis; D011549:Pseudomonas / Q000201:enzymology*; D013053:Spectrophotometry; D013552:Swine
D000596:Amino Acids; D046911:Macromolecular Substances; D005182:Flavin-Adenine Dinucleotide; D010088:Oxidoreductases; C021551:mercuric reductase; D008058:Dihydrolipoamide Dehydrogenase; D005980:Glutathione Reductase