Results 31 to 40 of about 10,826 (186)

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, R, Eisenthal, S, Hall, S R, Kessell, D L, Williams   +4 more
openaire   +2 more sources

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 ...
Ewa M, Ciszak, Anna, Makal, Young S, Hong, Ananthalakshmy K, Vettaikkorumakankauv, Lioubov G, Korotchkina, Mulchand S, Patel   +5 more
openaire   +2 more sources

Differences in gene expression of enzymes involved in branched-chain amino acid metabolism of abdominal subcutaneous adipose tissue between pregnant women with and without PCOS

Taiwanese Journal of Obstetrics & Gynecology, 2021
Objective: Polycystic ovary syndrome (PCOS) appears to be a common endocrine disorder of women in reproductive age. Adipose tissue (AT) is known as an active tissue in the metabolism of branched-chain amino acids (BCAA; Valine, Leucine, and Isoleucine ...
Shekoufeh Hajitarkhani, Ashraf Moini, Maryam Hafezi, Maryam Shahhoseini, AliReza Alizadeh   +4 more
doaj   +1 more source

Cryptic proteolytic activity of dihydrolipoamide dehydrogenase [PDF]

Proceedings of the National Academy of Sciences, 2007
The mitochondrial enzyme, dihydrolipoamide dehydrogenase (DLD), is essential for energy metabolism across eukaryotes. Here, conditions known to destabilize the DLD homodimer enabled the mouse, pig, or human enzyme to function as a protease. A catalytic dyad (S456–E431) buried at the homodimer interface was identified.
Ngolela Esther, Babady, Yuan-Ping, Pang, Orly, Elpeleg, Grazia, Isaya   +3 more
openaire   +2 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   +10 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

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

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

Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly [PDF]

, 2011
The final version of this article is available at the link below.Crucial to glucose homoeostasis in humans, the hPDC (human pyruvate dehydrogenase complex) is a massive molecular machine comprising multiple copies of three distinct enzymes (E1–E3) and an
Alan Cooper, Blass, Brautigam, Brautigam, Chamberlain, Ciszak, Cooper, David Gilbert, Donna P. McGow, Frank, Hipps, Hiromasa, Hodgson, Hoyer, Huang, Izard, J. Gordon Lindsay, Jones, Jung, Konarev, Laue, Lessard, Leung, Lynch, Mande, Margaret A. Nutley, Mayers, McCartney, Olwyn Byron, Peter Kropholler, Philip Callow, Robinson, Sanderson, Schuck, Semenyuk, Smolle, Stanley, Stoops, Svergun, Swetha Vijayakrishnan, Vijayakrishnan, Wagenknecht, Yu, Zhou, Zhou   +44 more
core   +3 more sources

Richard Nelson Perham. 27 April 1937—14 February 2015 [PDF]

, 2018
Richard Nelson Perham, FRS, FMedSci, FRSA, was a British professor of structural biochemistry. He undertook his academic career at the University of Cambridge, holding positions as lecturer, reader, chair and head of the Department of Biochemistry, as ...
Charoy, François, Ferme, Vincenzo, Labba, Chahrazed, On the Move toMeaningful Internet Systems, Pautasso, Cesare, Rosinosky, Guillaume, Youcef, Samir   +6 more
core   +3 more sources