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Proton translocating NAD(P) + transhydrogenase is one of the main ways that cells can regenerate NADPH after it is used. In E. coli, this pathway contribute equal amounts of NADPH as the pentose phosphate pathway, and both were the main producers of NADPH under standard growth conditions.
In biochemistry, NAD(P) + transhydrogenase (Si-specific) (EC 1.6.1.1) is an enzyme that catalyzes the chemical reaction. NADPH + NAD + NADP + + NADH. Thus, the two substrates of this enzyme are NADPH and NAD +, whereas its two products are NADP + and NADH. This enzyme participates in nicotinate and nicotinamide metabolism.
Transhydrogenase may stand for NAD(P)+ transhydrogenase (Re/Si-specific) NAD(P)+ transhydrogenase (Si-specific) Proton-Translocating NAD(P)+ Transhydrogenase; Hydroxyacid-oxoacid transhydrogenase; Glutathione—cystine transhydrogenase; Lactate—malate transhydrogenase; Glutathione—homocystine transhydrogenase; Glutathione—CoA-glutathione ...
NAD(P) transhydrogenase, mitochondrial is an enzyme that in humans is encoded by the NNT gene on chromosome 5. [5] [6] [7] The NNT gene contains 26 exons and encodes a transhydrogenase protein that is ~109 kDa in molecular weight and is involved in antioxidant defense in the mitochondria. Two alternatively spliced variants, encoding the same ...
This list contains a list of sub-classes for the seventh group of Enzyme Commission numbers, EC 7, translocases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
NAD(P)+ transhydrogenase (Si-specific) This page was last edited on 28 May 2015, at 13:20 (UTC). Text is available under the Creative Commons Attribution ...
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source').
NAD(P)+ transhydrogenase (Si-specific) This page was last edited on 28 May 2015, at 13:18 (UTC). Text is available under the Creative Commons Attribution ...