Integrate in silico studies on the role of nicotinamide adenine dinucleotide (NADH) binding in activating C-terminal binding protein 2 (CtBP2)

2021 ◽  
Author(s):  
Tsukasa Aoyagi ◽  
Ryunosuke Yoshino ◽  
Yuki Mitsuta ◽  
Rikuri Morita ◽  
Ryuhei Harada ◽  
...  
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
In Silico ◽  
Binding Protein ◽  
Nicotinamide Adenine ◽  
In Silico Studies

scholarly journals Cellular and mitochondrial mechanisms of atrial fibrillation

2020 ◽  
Vol 115 (6) ◽  
Author(s):  
Fleur E. Mason ◽  
Julius Ryan D. Pronto ◽  
Khaled Alhussini ◽  
Christoph Maack ◽  
Niels Voigt
Keyword(s):  
Atrial Fibrillation ◽  
Nicotinamide Adenine Dinucleotide ◽  
Molecular Mechanisms ◽  
Treatment Options ◽  
Specific Treatment ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Mitochondrial Activity ◽  
Atp Production

AbstractThe molecular mechanisms underlying atrial fibrillation (AF), the most common form of arrhythmia, are poorly understood and therefore target-specific treatment options remain an unmet clinical need. Excitation–contraction coupling in cardiac myocytes requires high amounts of adenosine triphosphate (ATP), which is replenished by oxidative phosphorylation in mitochondria. Calcium (Ca2+) is a key regulator of mitochondrial function by stimulating the Krebs cycle, which produces nicotinamide adenine dinucleotide for ATP production at the electron transport chain and nicotinamide adenine dinucleotide phosphate for the elimination of reactive oxygen species (ROS). While it is now well established that mitochondrial dysfunction plays an important role in the pathophysiology of heart failure, this has been less investigated in atrial myocytes in AF. Considering the high prevalence of AF, investigating the role of mitochondria in this disease may guide the path towards new therapeutic targets. In this review, we discuss the importance of mitochondrial Ca2+ handling in regulating ATP production and mitochondrial ROS emission and how alterations, particularly in these aspects of mitochondrial activity, may play a role in AF. In addition to describing research advances, we highlight areas in which further studies are required to elucidate the role of mitochondria in AF.

scholarly journals Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B

Blood ◽  
1995 ◽  
Vol 85 (1) ◽  
pp. 264-267 ◽  
Author(s):  
L Camardella ◽  
V Carratore ◽  
MA Ciardiello ◽  
G Damonte ◽  
U Benatti ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nicotinamide Adenine Dinucleotide ◽  
Stop Codon ◽  
Binding Protein ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Tumor Cell Line ◽  
Nicotinamide Adenine ◽  
Transplantation Antigen ◽  
Tryptic Peptides ◽  
Putative Protein

Human erythrocytes contain a nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein, FX, whose levels are significantly increased in erythrocytes from glucose-6-phosphate dehydrogenase (G6PD)- deficient individuals bearing the mediterranean variant of G6PD. Elucidation of the still unknown biologic functions of FX was approached by means of amino acid sequencing of its 25 tryptic peptides. Searching in the EMBL data bank allowed identification of extensive homology between these tryptic peptides and all sequence- aligned regions encompassing the complete structure of a putative protein encoded by the P35B gene in the mouse. This gene, which differs from the normal allele by a point mutation, has been previously cloned from a tum- variant of the murine tumor cell line P815, so defined because it is associated with low tumorigenicity compared with the progenitor P815. The reported P35B cDNA contains an open reading frame (ORF) of 813 bp and encodes a putative protein of 271 amino acids (30 kD), whereas FX protein is 320 amino acids in length (35.81 kD, in good agreement with previous studies). However, a single base shift at position 4,752 of the P35B gene suppresses the stop codon after Phe 271 and allows continuation of the ORF for up to 320 amino acids to reach the same length as FX. The remarkably high extent (92%) of homology indicates that erythrocyte FX protein is the human homolog of the P35B gene product.

scholarly journals Nicotinamide adenine dinucleotide as a photocatalyst

2019 ◽  
Vol 5 (7) ◽  
pp. eaax0501 ◽  
Author(s):  
Jinhyun Kim ◽  
Sahng Ha Lee ◽  
Florian Tieves ◽  
Caroline E. Paul ◽  
Frank Hollmann ◽  
...  
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Metallic Nanoparticles ◽  
Chemical Conversion ◽  
Nicotinamide Adenine ◽  
Traditional Role ◽  
Life Span Extension ◽  
Redox Biocatalysis ◽  
Total Turnover ◽  
Prosthetic Groups

Nicotinamide adenine dinucleotide (NAD+) is a key redox compound in all living cells responsible for energy transduction, genomic integrity, life-span extension, and neuromodulation. Here, we report a new function of NAD+ as a molecular photocatalyst in addition to the biological roles. Our spectroscopic and electrochemical analyses reveal light absorption and electronic properties of two π-conjugated systems of NAD+. Furthermore, NAD+ exhibits a robust photostability under UV-Vis-NIR irradiation. We demonstrate photocatalytic redox reactions driven by NAD+, such as O2 reduction, H2O oxidation, and the formation of metallic nanoparticles. Beyond the traditional role of NAD+ as a cofactor in redox biocatalysis, NAD+ executes direct photoactivation of oxidoreductases through the reduction of enzyme prosthetic groups. Consequently, the synergetic integration of biocatalysis and photocatalysis using NAD+ enables solar-to-chemical conversion with the highest-ever-recorded turnover frequency and total turnover number of 1263.4 hour−1 and 1692.3, respectively, for light-driven biocatalytic trans-hydrogenation.

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