Results 121 to 130 of about 1,484 (136)

Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)

Biochemistry, 1993
The catalytic domain of dihydrolipoyl transacetylase (E2pCD) forms the core of the pyruvate dehydrogenase multienzyme complex and catalyzes the acetyltransferase reaction using acetylCoA as acetyl donor and dihydrolipoamide (Lip(SH)2) as acceptor.
Andrea Mattevi, G. Obmolova, Kor H. Kalk, A. Teplyakov, W.G.J. Hol   +4 more
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The quaternary structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii

European Journal of Biochemistry, 1989
After limited proteolysis of the dihydrolipoyl transacetylase component (E2) of Azotobacter vinelandii pyruvate dehydrogenase complex (PDC), a C-terminal domain was obtained which retained the transacetylase active site and the quaternary structure of E2
Roeland Hanemaaijer, Adrie H. Westphal, T Heiden, Arie de KOK, C. Veeger   +4 more
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Heterogeneity of binding sites for the pyruvate dehydrogenase component on the dihydrolipoyl transacetylase core of bovine kidney pyruvate dehydrogenase complex

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 ...
Douglas R. Brandt, Thomas E. Roche, Mary L. Pratt   +2 more
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The catalytic domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex From Azotobacter vinelandii and Escherichia coli. Expression, purification, properties and preliminary X-ray analysis

European Journal of Biochemistry, 1991
Partial sequences of the dihydrolipoyl transacetylase component (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.
Egbert Schulze, Adrie H. Westphal, G. Obmolova, Andrea Mattevi, Wim G. J. Hol, Arie de KOK   +5 more
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Dissociation and Reassembly of the Dihydrolipoyl Transacetylase Component of the Bovine Heart Pyruvate Dehydrogenase Complex

Archives of Biochemistry and Biophysics, 1995
The catalytic activity and the state of aggregation of the dihydrolipoyl transacetylase-lipoamide dehydrogenase binding protein (E2-E3BP) subcomplex of the bovine heart pyruvate dehydrogenase multienzyme complex were investigated.
Olga L. De Marcucci, Michael S. DeBuysere, Merle S. Olson   +2 more
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Sizing of bovine heart and kidney pyruvate dehydrogenase complex and dihydrolipoyl transacetylase core by quasielastic light scattering

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
T.E. Roche, SUSAN L. POWERS‐GREENWOOD, Wen‐Jing Shi, W. B. Zhang, Shisong Ren, E. D. Roche, Daniel J. Cox, C. M. Sorensen   +7 more
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Dihydrolipoyl transacetylase

Enzyme Active Sites and their Reaction Mechanisms, 2020
Harry Morrison
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Cryo-EM structure of the dihydrolipoyl transacetylase cubic core of the E. coli pyruvate dehydrogenase complex including lipoyl domains

, 2020
Jana Škerlová, Pål Stenmark
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Crystallization of a dihydrolipoyl transacetylase-dihydrolipoyl dehydrogenase subcomplex and its implications regarding the subunit structure of the pyruvate dehydrogenase complex from Escherichia coli

Biochemical and Biophysical Research Communications - BBRC, 1979
Charles C. Fuller, Lester J. Reed, Robert M. Oliver, Marvin L. Hackert   +3 more
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The pyruvate dehydrogenase complex from the parasitic nematode Ascaris suum: Novel subunit composition and domain structure of the dihydrolipoyl transacetylase component

Archives of Biochemistry and Biophysics, 1992
Richard Komuniecki, Robert Y. Rhee, Deepashree Bhat, Emilio Duran, Emil Sidawy, Hebok Song   +5 more
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