Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases |
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| Authors: | R Delaney G Burns J R Sokatch |
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| Affiliation: | Unité de Biochimie Cellulaire, Département de Biochimie et Génétique Moléculaire, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France |
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| Abstract: | 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. |
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| Keywords: | Lipoamide dehydrogenase Branched-chain keto acid dehydrogenase To whom correspondence should be addressed |
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