(Q28187388)

English

Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components

scientific article (publication date: 20 February 2004)

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scholarly article

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Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components (English)

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author name string

Yasuaki Hiromasa

1

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Tetsuro Fujisawa

2

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Yoichi Aso

3

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Thomas E Roche

4

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language of work or name

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publication date

20 February 2004

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Journal of Biological Chemistry

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279

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6921-33

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8

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Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms

1 reference

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Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1.

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Component X. An immunologically distinct polypeptide associated with mammalian pyruvate dehydrogenase multi-enzyme complex.

1 reference

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Reconstitution of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes: analysis of protein X involvement and interaction of homologous and heterologous dihydrolipoamide dehydrogenases

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Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex

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Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae

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Functional analysis of the domains of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae

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Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae

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On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex

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Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex

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Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex

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Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes

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Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics

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Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile

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A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions.

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Analysis of weight average sedimentation velocity data

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Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase

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Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins.

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The effects of ionic strength on the self-association of human spectrin.

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Sizing of bovine heart and kidney pyruvate dehydrogenase complex and dihydrolipoyl transacetylase core by quasielastic light scattering.

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Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions

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The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes

1 reference

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

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Conformational flexibility of pyruvate dehydrogenase complexes: a computational analysis by quantized elastic deformational model

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21 January 2018

Identifiers

10.1074/JBC.M308172200

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