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Multienzyme complexes
1970
Reed, L.J.; Cox, D.J.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
1
213-240
Subunit composition and partial reactions of the 2-oxoglutarate dehydrogenase complex of Acetobacter xylinum
1980
De Kok, A.; Kornfeld, S.; Benziman, M.; Milner, Y.
Eur. J. Biochem.
106
49-58
alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex
1973
Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.
J. Biol. Chem.
248
5282-5290
Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex
1996
Hein, S.; Steinbuechel, A.
FEMS Microbiol. Lett.
136
231-238
Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex
1971
Derosier, D.J.; Oliver, R.M.; Reed, L.J.
Proc. Natl. Acad. Sci. USA
68
1135-1137
A continuous spectrophotometric assay for the transacylase (E2) component of pyruvate and alpha-oxoglutarate dehydrogenase enzyme complexes
1974
Hall, E.R.; Weitzman, P.D.J.
Anal. Biochem.
62
286-290
Mammalian alpha-keto acid dehydrogenase complexes. 8. Properties and subunit composition of the pig heart lipoate succinyltransferase
1974
Tanaka, N.; Koike, K.; Otsuka, K.I.; Hamada, M.; Ogasahara, K.; Koike, M.
J. Biol. Chem.
249
191-198
Structural and mechanistic studies of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli
1979
Angelides, K.J.; Hammes, G.G.
Biochemistry
18
5531-5537
Lipoic acid content of dihydrolipoyl transacylases determined by isotope dilution analysis
1980
White, R.H.; Bleile, D.M.; Reed, L.J.
Biochem. Biophys. Res. Commun.
94
78-84
Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
1992
Robien, M.A.; Clore, G.M.; Omichinski, J.G.; Perham, R.N.; Appella, E.; Sakaguchi, K.; Gronenborn, A.M.
Biochemistry
31
3463-3471
Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex
1994
Nakano, K.; Takase, C.; Sakamoto, T.; Nakagawa, S.; Inazawa, J.; Ohta, S.; Matuda, S.
Eur. J. Biochem.
224
179-189
Different distribution of dihydrolipoamide succinyltransferase, dihydrolipoamide acetyltransferase and ATP synthase beta-subunit in monkey brain
1996
Takase, C.; Nakano, K.; Ohta, S.; Nakagawa, S.; Matuda, S.
In Vivo
10
495-502
A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle
1997
Matuda, S.; Kodama, J.; Goshi, N.; Takase, C.; Nakano, K.; Nakagawa, S.; Ohta, S.
Biochem. Biophys. Res. Commun.
241
151-156
Immunoreactivity of porcine heart dihydrolipoamide acetyl- and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: characterization of the autoantigenic region and effects of enzymic delipoylation and relipoylation
1998
Koike, K.; Ishibashi, H.; Koike, M.
Hepatology
27
1467-1474
Characterization of the Coxiella burnetii sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase
1999
Nguyen, S.V.; To, H.; Yamaguchi, T.; Fukushi, H.; Hirai, K.
Microbiol. Immunol.
43
743-749
Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase
2000
Knapp, J.E.; Carroll, D.; Lawson, J.E.; Ernst, S.R.; Reed, L.J.; Hackert, M.L.
Protein Sci.
9
37-48
Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex
2000
Koike, K.; Suematsu, T.; Ehara, M.
Eur. J. Biochem.
267
3005-3016
Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein
2001
Zygmunt, M.S.; Diaz, M.A.; Teixeira-Gomes, A.P.; Cloeckaert, A.
Infect. Immun.
69
6537-6540
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