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Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.
ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3−-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.
ATP synthase is an enzyme that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is:
In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template.
Chemiosmosis is the movement of ions across a semipermeable membrane bound structure, down their electrochemical gradient. An important example is the formation of adenosine triphosphate (ATP) by the movement of hydrogen ions (H+) across a membrane during cellular respiration or photosynthesis.
DNA gyrase, or simply gyrase, is an enzyme within the class of topoisomerase and is a subclass of Type II topoisomerases that reduces topological strain in an ATP dependent manner while double-stranded DNA is being unwound by elongating RNA-polymerase or by helicase in front of the progressing replication fork. It is the only known enzyme to actively contribute negative supercoiling to DNA, while it also is capable of relaxing positive supercoils. It does so by looping the template to form a crossing, then cutting one of the double helices and passing the other through it before releasing the break, changing the linking number by two in each enzymatic step. This process occurs in bacteria, whose single circular DNA is cut by DNA gyrase and the two ends are then twisted around each other to form supercoils. Gyrase is also found in eukaryotic plastids: it has been found in the apicoplast of the malarial parasite Plasmodium falciparum and in chloroplasts of several plants. Bacterial DNA gyrase is the target of many antibiotics, including nalidixic acid, novobiocin, albicidin, and ciprofloxacin.
Tibotec was a pharmaceutical company with a focus on research and development for the treatment of infectious diseases such as HIV/AIDS and hepatitis C. The company was founded in 1994 and then acquired by Johnson & Johnson and merged into its Janssen Pharmaceuticals division in 2002.
Glycogen synthase is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase that catalyses the reaction of UDP-glucose and n to yield UDP and n+1.
The rpoB gene encodes the β subunit of bacterial RNA polymerase and the homologous plastid-encoded RNA polymerase (PEP). It codes for 1342 amino acids in E. coli, making it the second-largest polypeptide in the bacterial cell. It is targeted by the rifamycin family of antibacterials, such as rifampin. Mutations in rpoB that confer resistance to rifamycins do so by altering the protein's drug-binding residues, thereby reducing affinity for these antibiotics.
In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. It typically uses malonyl-CoA as a carbon source to elongate ACP-bound acyl species, resulting in the formation of ACP-bound β-ketoacyl species such as acetoacetyl-ACP.
Bedaquiline, sold under the brand name Sirturo, is a medication used to treat active tuberculosis. Specifically, it is used to treat multi-drug-resistant tuberculosis (MDR-TB) along with other medications for tuberculosis. It is used by mouth.
Aminocoumarin is a class of antibiotics that act by an inhibition of the DNA gyrase enzyme involved in the cell division in bacteria. They are derived from Streptomyces species, whose best-known representative – Streptomyces coelicolor – was completely sequenced in 2002. The aminocoumarin antibiotics include:
Isocitrate lyase, or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle and is used by bacteria, fungi, and plants.
ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals represents an important step in fatty acid biosynthesis. By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA. In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.
In enzymology, a β-ketoacyl-[acyl-carrier-protein] synthase III (EC 2.3.1.180) is an enzyme that catalyzes the chemical reaction
In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction
ATP synthase-coupling factor 6, mitochondrial is an enzyme subunit that in humans is encoded by the ATP5PF gene.
ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene.
Koen Andries is a Belgian Janssen Pharmaceutica scientist and professor at the University of Antwerp. In 2005 he and his team published a discovery about a new di-Aryl-Quinoline-based drug (R207910), now called bedaquiline, which promises a shorter and simpler treatment for drug resistant Tuberculosis (TB).
Proteasomeaccessory factor E is an ATP-independent proteasome activator of Mycobacterium tuberculosis that forms 12-fold symmetric rings and interacts with the 20S proteasome core particle through a conserved carboxyl-terminal motif to activate peptide and protein degradation.
References
- ↑ Koul, Anil; Dendouga, Najoua; Vergauwen, Karen; Molenberghs, Brenda; Vranckx, Luc; Willebrords, Rudy; Ristic, Zorica; Lill, Holger; Dorange, Ismet; Guillemont, Jerome; Bald, Dirk; Andries, Koen (2007). "Diarylquinolines target subunit c of mycobacterial ATP synthase". Nature Chemical Biology. 3 (6): 323–324. doi:10.1038/nchembio884. ISSN 1552-4450. PMID 17496888.
- 1 2 Haagsma, A. C.; Abdillahi-Ibrahim, R.; Wagner, M. J.; Krab, K.; Vergauwen, K.; Guillemont, J.; Andries, K.; Lill, H.; Koul, A.; Bald, D. (2008). "Selectivity of TMC207 towards Mycobacterial ATP Synthase Compared with That towards the Eukaryotic Homologue" (PDF). Antimicrobial Agents and Chemotherapy. 53 (3): 1290–2. doi:10.1128/AAC.01393-08. PMC 2650532 . PMID 19075053.
- ↑ Wang, Xiang-Shan; Zhang, Mei-Mei; Jiang, Hong; Yao, Chang-Sheng; Tu, Shu-Jiang (2008). "Uncatalyzed and Solvent-Free Process for the Synthesis of 1,4-Diarylquinoline Derivatives". Synthetic Communications. 38 (9): 1355–1364. doi:10.1080/00397910801916397.
- ↑ Metal free synthesis of 2,4-diarylquinoline derivatives with enamides and imines