Results 131 to 140 of about 4,093 (168)

Protein lipoylation: mitochondria, cuproptosis, and beyond

Trends in Biochemical Sciences
Protein lipoylation, a crucial post-translational modification (PTM), plays a pivotal role in mitochondrial function and emerges as a key player in cell death through cuproptosis. This novel copper-driven cell death pathway is activated by excessive copper ions binding to lipoylated mitochondrial proteins, disrupting energy production and causing ...
Cheng-Han Lin, Yeh Chin, Ming Zhou, Robert W. Sobol, Mien-Chie Hung, Ming Tan   +5 more
openaire   +2 more sources

A Lipoate-Protein Ligase Is Required for De Novo Lipoyl-Protein Biosynthesis in the Hyperthermophilic Archaeon Thermococcus kodakarensis

Applied and Environmental Microbiology, 2022
Based on previous studies in bacteria and eukaryotes, lipoate-protein ligases (Lpls) have been considered to be involved exclusively in lipoate salvage. The genetic analyses in this study on the lipoate-protein ligase in T. kodakarensis , however, suggest otherwise and that the enzyme is additionally involved in
Jian-qiang Jin, Takaaki Sato, Shin-ichi Hachisuka, Haruyuki Atomi   +3 more
openaire   +2 more sources

[32] Assay for protein lipoylation reaction

1995
Publisher Summary This chapter discusses the assay for protein lipoylation reaction. Lipoate attaches to the ɛ -amino group of the specific lysine residue of the proteins via an amide linkage. The lipoyllysine residue functions as a carrier of intermediates of the reactions and reducing equivalents between the active sites of the components of the ...
Kazuko Fujiwara, Kazuko Okamura-Ikeda, Yutaro Motokawa   +2 more
openaire   +1 more source

Escherichia coli LipA Is a Lipoyl Synthase:  In Vitro Biosynthesis of Lipoylated Pyruvate Dehydrogenase Complex from Octanoyl-Acyl Carrier Protein

Biochemistry, 2000
The Escherichia coli lipA gene product has been genetically linked to carbon-sulfur bond formation in lipoic acid biosynthesis [Vanden Boom, T. J., Reed, K. E., and Cronan, J. E., Jr. (1991) J. Bacteriol. 173, 6411-6420], although in vitro lipoate biosynthesis with LipA has never been observed.
J R, Miller, R W, Busby, S W, Jordan, J, Cheek, T F, Henshaw, G W, Ashley, J B, Broderick, J E, Cronan, M A, Marletta   +8 more
openaire   +2 more sources

[FeFe]‐Hydrogenase: Defined Lysate‐Free Maturation Reveals a Key Role for Lipoyl‐H‐Protein in DTMA Ligand Biosynthesis

Angewandte Chemie International Edition, 2022
AbstractMaturation of [FeFe]‐hydrogenase (HydA) involves synthesis of a CO, CN−, and dithiomethylamine (DTMA)‐coordinated 2Fe subcluster that is inserted into HydA to make the active hydrogenase. This process requires three maturation enzymes: the radical S‐adenosyl‐l‐methionine (SAM) enzymes HydE and HydG, and the GTPase HydF. In vitro maturation with
Adrien Pagnier, Batuhan Balci, Eric M. Shepard, Hao Yang, Douglas M. Warui, Stella Impano, Squire J. Booker, Brian M. Hoffman, William E. Broderick, Joan B. Broderick   +9 more
openaire   +2 more sources

Phylogenetic and immunological definition of four lipoylated proteins from Novosphingobium aromaticivorans, implications for primary biliary cirrhosis

Journal of Autoimmunity, 2005
Novosphingobium aromaticivorans, a unique ubiquitous bacterium that metabolizes xenobiotics and activates environmental estrogens, has been suggested as a pathogenic factor in the development of primary biliary cirrhosis (PBC). To define the molecular basis of PBC sera reactivity, we investigated the characteristic of the bacterial antigens involved ...
K. A. Padgett, C. Selmi, T. P. Kenny, P. S. Leung, D. L. Balkwill, A. A. Ansari, R. L. Coppel, M. E. Gershwin   +7 more
openaire   +3 more sources

Pyruvate dehydrogenase complex from the primitive insect trypanosomatid, Crithidia fasciculata: dihydrolipoyl dehydrogenase-binding protein has multiple lipoyl domains

Molecular and Biochemical Parasitology, 1995
The pyruvate dehydrogenase complex (PDC) has been purified to apparent homogeneity from the insect trypanosomatid, Crithidia fasciculata, a member of the most primitive eukaryotic group to contain mitochondria. Separation of the purified PDC by SDS-PAGE yielded five bands of 70 (p70), 60 (p60), 55, 46 and 36.5 kDa, which appeared to correspond to ...
F, Diaz, R, Komuniecki
openaire   +2 more sources

Defect in the lipoyl-bearing protein X subunit of the pyruvate dehydrogenase complex in two patients with encephalomyelopathy

The Journal of Pediatrics, 1993
Among the many metabolic encephalomyelopathies caused by deficiencies in the pyruvate dehydrogenase complex (PDHC), nearly all involve its E1 subunit. We describe two new familial cases of PDHC deficiency with encephalomyelopathy, chronic lactic acidemia, and a normal E1 subunit of PDHC but deficiency in another component. Activity of PDHC was measured
C, Marsac, D, Stansbie, G, Bonne, J, Cousin, P, Jehenson, C, Benelli, J P, Leroux, G, Lindsay   +7 more
openaire   +2 more sources

Lipoyl dehydrogenase catalyzes reduction of nitrated DNA and protein adducts using dihydrolipoic acid or ubiquinol as the cofactor

Chemico-Biological Interactions, 2002
Inflamed tissues generate reactive nitrogen oxide species (RNO(x)), such as peroxynitrite (ONOO-)and nitryl chloride (NO2Cl), which lead to formation of nitrated DNA and protein adducts, including 8-nitroguanine (8NG), 8-nitroxanthine (8NX), and 3-nitrotyrosine (3NT).
Hauh-Jyun Candy, Chen, Yuan-Mao, Chen, Chia-Ming, Chang   +2 more
openaire   +2 more sources

Oligocopper‐Loaded Lipoic Acid Nanoparticles Promote Mitochondrial Protein Lipoylation for Augmented Cuproptosis Therapy

Small
Abstract Cuproptosis is a modality of mitochondrial cell death driven by the binding of excess copper ions to the lipoic acid residues of dihydrolipoamide S‐acetyltransferase (DLAT) protein. However, copper levels are tightly regulated within cells. Herein, an oligocopper‐loaded lipoic acid nanoparticle (Cu@TcNAs)
Ying Chen, Junyu Wang, Yaya Zheng, Jun Zhang, Juan Wang, Haoran Ye, Ling Tao, Yongchao Yao, Xinghong Luo, Yang Ding, Xiangchun Shen   +10 more
openaire   +1 more source