Results 131 to 140 of about 746 (145)
Biochemistry, 1983 We have characterized the dissociation equilibrium constant (Kd) and the rate constants of association and dissociation for the binding of the pyruvate dehydrogenase component (PDH) to the dihydrolipoyl transacetylase component of kidney pyruvate dehydrogenase complex.
Douglas R. Brandt +2 more
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Biochemistry, 1993 Quasielastic light scattering (QELS) measurements on several preparations of bovine heart and kidney pyruvate dehydrogenase complex yielded hydrodynamic radii (rH values) ranging from 25.7 to 30 nm. Gel filtration chromatography removed stable aggregates and generated preparations that gave essentially the same rH values of 24.3 +/- 0.6 nm for both ...
T.E. Roche +7 more
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European Journal of Biochemistry, 1991 Partial sequences of the dihydrolipoyl transacetylase componenent (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli, containing the catalytic domain, were cloned in pUC plasmids and over‐expressed in E. coli TG2.
Egbert Schulze +5 more
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Archives of Biochemistry and Biophysics, 1992 The pyruvate dehydrogenase complex (PDC) from muscle of the adult parasitic nematode Ascaris suum plays a unique role in its anaerobic mitochondrial metabolism. Resolution of the intact complex in high salt dissociates the pyruvate dehydrogenase subunit but leaves the dihydrolipoyl dehydrogenase subunit (E3) and two other proteins with apparent M(r)s ...
Richard Komuniecki +5 more
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Dihydrolipolyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide
Biochemistry, 1986The dihydrolipoyl transacetylase component (E2) of the pyruvate dehydrogenase complex catalyzes the reaction of acetyl coenzyme A (acetyl-CoA) with dihydrolipoamide, producing coenzyme A and S-acetyldihydrolipoamide. The acetyl group is shown by experiments reported herein to be bonded to S8 in the enzymatic product.
Y S, Yang, P A, Frey
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