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Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)
Biochemistry, 1993The 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. The crystal structures of six complexes and derivatives of Azotobacter vinelandii E2pCD were solved.
MATTEVI, ANDREA +4 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.
Yuh-Shyong Yang, Perry A. Frey
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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. Treatment of E2-E3BP with the chaotropic salts GndnCl or KSCN led to a rapid decrease in transacetylase activity which was ...
Olga G. L. De Marcucci +2 more
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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. Treatment of E2-E3BP with the chaotropic salts GndnCl or KSCN led to a rapid decrease in transacetylase activity which was ...
Olga G. L. De Marcucci +2 more
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Journal of Biochemical and Biophysical Methods, 1982
The dihydrolipoyl transacetylase core components of the bovine kidney and heart pyruvate dehydrogenase complexes were covalently attached through the lipoyl moiety to Sepharose by the thiol-crosslinking reagent, N,N'-p-phenylenedimaleimide. In one approach, the N,N-p-phenylenedimaleimide was allowed to react with glutathione which was in turn linked by
Thomas E. Roche +2 more
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The dihydrolipoyl transacetylase core components of the bovine kidney and heart pyruvate dehydrogenase complexes were covalently attached through the lipoyl moiety to Sepharose by the thiol-crosslinking reagent, N,N'-p-phenylenedimaleimide. In one approach, the N,N-p-phenylenedimaleimide was allowed to react with glutathione which was in turn linked by
Thomas E. Roche +2 more
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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 but had lost the lipoyl‐containing N‐terminal part of the chain and the binding sites for the ...
Hanemaaijer, R. +4 more
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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 but had lost the lipoyl‐containing N‐terminal part of the chain and the binding sites for the ...
Hanemaaijer, R. +4 more
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Journal of Molecular Biology, 1993
Dihydrolipoyl transacetylase (E2p) is both structurally and functionally the central enzyme of the pyruvate dehydrogenase multienzyme complex. The crystal structure of the catalytic domain, i.e. residues 382 to 637, of Azotobacter vinelandii E2p (E2pCD) was solved by multiple isomorphous replacement and refined by energy minimization procedures.
MATTEVI, ANDREA +5 more
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Dihydrolipoyl transacetylase (E2p) is both structurally and functionally the central enzyme of the pyruvate dehydrogenase multienzyme complex. The crystal structure of the catalytic domain, i.e. residues 382 to 637, of Azotobacter vinelandii E2p (E2pCD) was solved by multiple isomorphous replacement and refined by energy minimization procedures.
MATTEVI, ANDREA +5 more
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Biochemical and Biophysical Research Communications, 1979
Abstract A subcomplex consisting of dihydrolipoyl transacetylase and dihydrolipoyl dehydrogenase, two of the three enzymes comprising the Escherichia coli pyruvate dehydrogenase complex, has been crystallized. X-ray diffraction data establish that the space group is P 2 1 3 with unit cell dimension a=211 .5 A .
Robert M. Oliver +3 more
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Abstract A subcomplex consisting of dihydrolipoyl transacetylase and dihydrolipoyl dehydrogenase, two of the three enzymes comprising the Escherichia coli pyruvate dehydrogenase complex, has been crystallized. X-ray diffraction data establish that the space group is P 2 1 3 with unit cell dimension a=211 .5 A .
Robert M. Oliver +3 more
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