Results 1 to 10 of about 52 (52)

Mitochondrial transport and metabolism of the vitamin B‐derived cofactors thiamine pyrophosphate, coenzyme A, FAD and NAD+, and related diseases: A review

IUBMB Life, Volume 74, Issue 7, Page 592-617, July 2022., 2022
Abstract Multiple mitochondrial matrix enzymes playing key roles in metabolism require cofactors for their action. Due to the high impermeability of the mitochondrial inner membrane, these cofactors need to be synthesized within the mitochondria or be imported, themselves or one of their precursors, into the organelles.
Ferdinando Palmieri, Magnus Monné, Giuseppe Fiermonte, Luigi Palmieri   +3 more
wiley   +1 more source

Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli [PDF]

Proceedings of the National Academy of Sciences, 1979
Limited tryptic digestion of the pyruvate dehydrogenase complex of Escherichia coli or its dihydrolipoyl transacetylase core cleaves the trypsin-sensitive transacetylase subunits into two large fragments, A (lipoyl domain) and D (subunit binding domain). Release of fragments A from the complex does not significantly
Robert M. Oliver, Lester J. Reed, Dennis M. Bleile, Peter Munk   +3 more
openaire   +3 more sources

Identification of PDHX as a metabolic target for esophageal squamous cell carcinoma

Cancer Science, Volume 112, Issue 7, Page 2792-2802, July 2021., 2021
Inoue et al. found that pyruvate dehydrogenase (PDH) component X expression is necessary for PDH activity and is involved in the cancer stemness of esophageal squamous cell carcinoma (ESCC) cells, thereby being metabolically essential for the tumor growth of ESCC.
Jun Inoue, Masahiro Kishikawa, Hitoshi Tsuda, Yasuaki Nakajima, Takahiro Asakage, Johji Inazawa   +5 more
wiley   +1 more source

The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1987
Limited proteolysis with trypsin has been used to study the domain structure of the dihydrolipoyltransacetylase (E2) component of the pyruvate dehydrogenase complex of Azotobacter vinelandii. Two stable end products were obtained and identified as the N-terminal lipoyl domain and the C-terminal catalytic domain.
Hanemaaijer, R., de Kok, A., Jolles, J., Veeger, C.   +3 more
openaire   +4 more sources

The gene encoding dihydrolipoyl transacetylase from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1989
The gene encoding the dihydrolipoyl transacetylase (E2) component from Azotobacter vinelandii has been cloned in Escherichia coli. High expression of the gene was found when the cells were grown for more than 14 h. The E2 produced was partially active, varying 10 and 90% in different experiments.
Hanemaaijer, R., Westphal, A.H., Berg, A., van Dongen, W.M.A.M., de Kok, A., Veeger, C.   +5 more
openaire   +4 more sources

Interaction of lipoamide dehydrogenase with the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

European Journal of Biochemistry, 1991
The interaction between lipoamide dehydrogenase (E3) and dihydrolipoyl transacetylase (E2p) from the pyruvate dehydrogenase complex was studied during the reconstitution of monomeric E3 apoenzymes from Azotobacter vinelandii and Pseudomonas fluorescens.
Schulze, E., Benen, J.A.E., Westphal, A.H., de Kok, A.   +3 more
openaire   +3 more sources

A kinetic study of dihydrolipoyl transacetylase from bovine kidney.

Journal of Biological Chemistry, 1975
The mammalian pyruvate dehydrogenase complex contains a core, consisting of dihydrolipoyl transacetylase, to which pyruvate dehydrogenase and dihydrolipoyl dehydrogenase are joined. This report describes studies on the kinetic mechanism of the transacetylase-catalyzed reaction between [1-14C]acetyl-CoA and dihydrolipoamide.
M H Eley, Thomas E. Roche, C S Tsai, Peter J. Butterworth, Lester J. Reed   +4 more
openaire   +3 more sources

In vitro reconstitution and characterization of pyruvate dehydrogenase and 2‐oxoglutarate dehydrogenase hybrid complex from Corynebacterium glutamicum

MicrobiologyOpen, Volume 9, Issue 10, October 2020., 2020
This study shows the unique molecular architecture of the PDH‐ODH hybrid complex in Corynebacterium glutamicum, in which both CgE1p and CgE1o associate with the CgE2‐E3 subcomplex. The core‐forming CgE2‐E3 probably consists of six copies of CgE2, which is relatively compact compared with PDH and ODH in other microorganisms that have 24 copies of E2 ...
Hirokazu Kinugawa, Naoko Kondo, Ayano Komine‐Abe, Takeo Tomita, Makoto Nishiyama, Saori Kosono   +5 more
wiley   +1 more source

Nematode pyruvate dehydrogenase kinases: role of the C-terminus in binding to the dihydrolipoyl transacetylase core of the pyruvate dehydrogenase complex [PDF]

Biochemical Journal, 1999
Pyruvate dehydrogenase kinases (PDKs) from the anaerobic parasitic nematode Ascaris suum and the free-living nematode Caenorhabditis elegans were functionally expressed with hexahistidine tags at their N-termini and purified to apparent homogeneity. Both recombinant PDKs (rPDKs) were dimers, were not autophosphorylated and exhibited similar specific ...
Patricia R. Komuniecki, Richard Komuniecki, Wei Chen   +2 more
openaire   +3 more sources

Time‐resolved fluorescence studies on the dihydrolipoyl transacetylase (E₂) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii [PDF]

FEBS Letters, 1988
The dihydrolipoyl transacetylase (E2) component of A. vinelandii PDC and its lipoyl domain shows similar dynamic properties as revealed with fluorescence anisotropy decay of lipoyl‐bound IAANS. The lipoyl domain (32.6 kDa), containing three almost identical subdomains shows a mode of rotation characteristic for a protein of about 30 kDa.
Hanemaaijer, Roeland, Masurel, Remco, Visser, Antonie J.W.G., de Kok, Arie, Veeger, Cees   +4 more
openaire   +2 more sources