Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases - PubMed (original) (raw)
Comparative Study
. 1984 Mar 26;168(2):265-70.
doi: 10.1016/0014-5793(84)80259-8.
- PMID: 6373365
- DOI: 10.1016/0014-5793(84)80259-8
Free article
Comparative Study
Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases
R Delaney et al. FEBS Lett. 1984.
Free article
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.
Similar articles
- Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida.
Burns G, Brown T, Hatter K, Sokatch JR. Burns G, et al. Eur J Biochem. 1989 Jan 15;179(1):61-9. doi: 10.1111/j.1432-1033.1989.tb14521.x. Eur J Biochem. 1989. PMID: 2917566 - Oxidation of glycine by Pseudomonas putida requires a specific lipoamide dehydrogenase.
Sokatch JR, Burns G. Sokatch JR, et al. Arch Biochem Biophys. 1984 Feb 1;228(2):660-6. doi: 10.1016/0003-9861(84)90036-5. Arch Biochem Biophys. 1984. PMID: 6546487 - Isolation of a third lipoamide dehydrogenase from Pseudomonas putida.
Burns G, Sykes PJ, Hatter K, Sokatch JR. Burns G, et al. J Bacteriol. 1989 Feb;171(2):665-8. doi: 10.1128/jb.171.2.665-668.1989. J Bacteriol. 1989. PMID: 2914869 Free PMC article. - Immunochemical relationships among pig heart lipoamide dehydrogenases.
Hayakawa T, Aikawa T, Otsuka K, Koike M. Hayakawa T, et al. J Biochem. 1967 Sep;62(3):396-7. J Biochem. 1967. PMID: 4171997 Review. No abstract available.
Cited by
- Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida.
Palmer JA, Hatter K, Sokatch JR. Palmer JA, et al. J Bacteriol. 1991 May;173(10):3109-16. doi: 10.1128/jb.173.10.3109-3116.1991. J Bacteriol. 1991. PMID: 1902462 Free PMC article. - Conjugative mapping of pyruvate, 2-ketoglutarate, and branched-chain keto acid dehydrogenase genes in Pseudomonas putida mutants.
Sykes PJ, Menard J, McCully V, Sokatch JR. Sykes PJ, et al. J Bacteriol. 1985 Apr;162(1):203-8. doi: 10.1128/jb.162.1.203-208.1985. J Bacteriol. 1985. PMID: 3980435 Free PMC article. - Isolation of an atypically small lipoamide dehydrogenase involved in the glycine decarboxylase complex from Eubacterium acidaminophilum.
Freudenberg W, Dietrichs D, Lebertz H, Andreesen JR. Freudenberg W, et al. J Bacteriol. 1989 Mar;171(3):1346-54. doi: 10.1128/jb.171.3.1346-1354.1989. J Bacteriol. 1989. PMID: 2537814 Free PMC article. - Molecular cloning of genes encoding branched-chain keto acid dehydrogenase of Pseudomonas putida.
Sykes PJ, Burns G, Menard J, Hatter K, Sokatch JR. Sykes PJ, et al. J Bacteriol. 1987 Apr;169(4):1619-25. doi: 10.1128/jb.169.4.1619-1625.1987. J Bacteriol. 1987. PMID: 3549697 Free PMC article. - Resolution of branched-chain oxo acid dehydrogenase complex of Pseudomonas aeruginosa PAO.
McCully V, Burns G, Sokatch JR. McCully V, et al. Biochem J. 1986 Feb 1;233(3):737-42. doi: 10.1042/bj2330737. Biochem J. 1986. PMID: 3085653 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources