Results 31 to 40 of about 9,205 (218)

How Dihydrolipoamide Dehydrogenase-binding Protein Binds Dihydrolipoamide Dehydrogenase in the Human Pyruvate Dehydrogenase Complex [PDF]

Journal of Biological Chemistry, 2006
The dihydrolipoamide dehydrogenase-binding protein (E3BP) and the dihydrolipoamide acetyltransferase (E2) component enzyme form the structural core of the human pyruvate dehydrogenase complex by providing the binding sites for two other component proteins, dihydrolipoamide dehydrogenase (E3) and pyruvate dehydrogenase (E1), as well as pyruvate ...
Mulchand S. Patel, Ewa Ciszak, Anna Makal, Lioubov G. Korotchkina, Ananthalakshmy K. Vettaikkorumakankauv, Young Soo Hong   +5 more
openaire   +3 more sources

The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression

Hepatology, EarlyView., 2022
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro, Rut Espinosa‐Sotelo, Eva Crosas‐Molist, Macarena Herranz‐Itúrbide, Daniel Caballero‐Díaz, Ania Alay, Xavier Solé, Emilio Ramos, Teresa Serrano, María L. Martínez‐Chantar, Ulla G. Knaus, José M. Cuezva, Antonio Zorzano, Esther Bertran, Isabel Fabregat   +14 more
wiley   +1 more source

Dihydrolipoamide dehydrogenase from halophilic archaebacteria [PDF]

Biochemical Journal, 1984
Dihydrolipoamide dehydrogenase has been discovered in the halophilic archaebacteria for the first time. The enzyme from both classical and alkaliphilic halobacteria has been investigated. (1) The enzyme specifically catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+.
M J Danson, S R Kessell, D L Williams, R Eisenthal, S Hall   +4 more
openaire   +3 more sources

The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens [PDF]

FEMS Microbiology Letters, 2008
A dihydrolipoamide dehydrogenase (DLDH) was purified and characterized for the first time from a crenarchaeon, Acidianus ambivalens. The holoenzyme consists of two identical subunits with a molecular mass of 45.4 kDa per monomer. It contains FAD as a prosthetic group and uses NAD+ as the preferential substrate, but can also reduce NADP+.
Arnulf Kletzin, Ana P. Batista, Manuela M. Pereira   +2 more
openaire   +3 more sources

Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism

IUCrJ, 2020
DHTKD1 is a lesser-studied E1 enzyme among the family of 2-oxoacid dehydrogenases. In complex with E2 (dihydrolipoamide succinyltransferase, DLST) and E3 (dihydrolipoamide dehydrogenase, DLD) components, DHTKD1 is involved in lysine and tryptophan ...
Gustavo A. Bezerra, William R. Foster, Henry J. Bailey, Kevin G. Hicks, Sven W. Sauer, Bianca Dimitrov, Thomas J. McCorvie, Jürgen G. Okun, Jared Rutter, Stefan Kölker, Wyatt W. Yue   +10 more
doaj   +1 more source

Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. [PDF]

Proceedings of the National Academy of Sciences, 1988
Rabbit antiserum to the dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC 1.8.1.4) component of the pyruvate dehydrogenase complex from bakers' yeast was used to screen plaques produced by a lambda gt11 yeast cDNA library.
Karen S. Browning, Lester J. Reed, David J. Uhlinger   +2 more
openaire   +3 more sources

Whole-genome sequence analysis of Bombella intestini LMG 28161T, a novel acetic acid bacterium isolated from the crop of a red-tailed bumble bee, Bombus lapidarius [PDF]

, 2016
The whole-genome sequence of Bombella intestini LMG 28161(T), an endosymbiotic acetic acid bacterium (AAB) occurring in bumble bees, was determined to investigate the molecular mechanisms underlying its metabolic capabilities.
Borremans, Wim, Cleenwerck, Ilse, De Vuyst, Luc, Illeghems, Koen, Li, Leilei, Smagghe, Guy, Van Kerrebroeck, Simon, Vandamme, Peter   +7 more
core   +9 more sources

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

MicrobiologyOpen, 2020
Pyruvate dehydrogenase (PDH) and 2‐oxoglutarate dehydrogenase (ODH) are critical enzymes in central carbon metabolism. In Corynebacterium glutamicum, an unusual hybrid complex consisting of CgE1p (thiamine diphosphate‐dependent pyruvate dehydrogenase ...
Hirokazu Kinugawa, Naoko Kondo, Ayano Komine‐Abe, Takeo Tomita, Makoto Nishiyama, Saori Kosono   +5 more
doaj   +1 more source

Protein–protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase [PDF]

Structure, 1996
The ubiquitous pyruvate dehydrogenase multienzyme complex is built around an octahedral or icosahedral core of dihydrolipoamide acetyltransferase (E2) chains, to which multiple copies of pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) bind tightly but non-covalently.
Sharmila S. Mande, Steve Sarfaty, Wim G. J. Hol, Mark D. Allen, Richard N. Perham   +4 more
openaire   +3 more sources

Change in Cofactor Specificity of Oxidoreductases by Adaptive Evolution of an Escherichia coli NADPH-Auxotrophic Strain

mBio, 2021
The nicotinamide cofactor specificity of enzymes plays a key role in regulating metabolic processes and attaining cellular homeostasis. Multiple studies have used enzyme engineering tools or a directed evolution approach to switch the cofactor preference
Madeleine Bouzon, Volker Döring, Ivan Dubois, Anne Berger, Gabriele M. M. Stoffel, Liliana Calzadiaz Ramirez, Sophia N. Meyer, Marion Fouré, David Roche, Alain Perret, Tobias J. Erb, Arren Bar-Even, Steffen N. Lindner   +12 more
doaj   +1 more source