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- W2360783669 abstract "Pyridine nucleotide transhydrogenases are the redox enzymes for directly catalyzing the reversible hydride transfer between NAD(H) and NADP(H), where they regulate and restore the homeostasis of those two redox cofactors in catabolism and anabolism. The membrane-bound pyridine nucleotide transhydrogenase (TH), ATP-linked transmembrane protein, is composed of two subunits, each of which contains three domains (dⅠ, dⅡ and dⅢ). TH drives the transfer of hydride from NADH to NADP~+ coupled with transmembrane proton import via binding-change catalytic mechanism. The soluble pyridine nucleotide transhydrogenase (STH) is energy-independent flavoprotein and form remarkably large polymers. Recently, it is considered that many mitochondrial diseases and cell damage caused by mitochondrial reactive oxygen species are related to TH activities, including diabetes, cancer, neurodegenerative diseases, cardiovascular diseases, and also apoptosis and aging. To investigate the molecular mechanism of TH may reveal the pathogenic mechanism of mitochondrial diseases and provide the molecular basis for diagnosis and gene therapy. Research of mechanism and utilization of STH in cofactor regenerating system may promote the further development of metabolic engineering and industrial biocatalysis process." @default.
- W2360783669 created "2016-06-24" @default.
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- W2360783669 date "2007-01-01" @default.
- W2360783669 modified "2023-09-23" @default.
- W2360783669 title "Structure and Function of Pyridine Nucleotide Transhydrogenases" @default.
- W2360783669 hasPublicationYear "2007" @default.
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