Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD‐linked dehydrogenases
- 26 March 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 168 (2) , 265-270
- https://doi.org/10.1016/0014-5793(84)80259-8
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.Keywords
This publication has 27 references indexed in Scilit:
- Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12European Journal of Biochemistry, 1983
- Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductaseBiochemistry, 1983
- Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptideBiochemistry, 1983
- Lipoamide Dehydrogenase from Baker’s Yeast. Improved Purification and Some Molecular, Kinetic, and Immunochemical PropertiesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Glutathione Reductase from Human Erythrocytes. Amino-Acid Sequence of the Structurally Known FAD-Binding DomainEuropean Journal of Biochemistry, 1981
- High performance liquid chromatographic determination of amino acids in the picomole rangeAnalytical Chemistry, 1979
- Glutathione Reductase from Human ErythrocytesEuropean Journal of Biochemistry, 1975
- Human Glutathione Reductase: Purification of the Crystalline Enzyme from ErythorocytesEuropean Journal of Biochemistry, 1974
- An amino acid sequence in the active site of lipoamide dehydrogenase from the 2‐oxoglutarate dehydrogenase complex ofE. coli (Crookes strain)FEBS Letters, 1972
- Estimation of Molecular Size and Molecular Weights of Biological Compounds by Gel FiltrationPublished by Wiley ,1970