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NADPH is used as a reducing agent in many anabolic reactions. 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 ...
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.
EC 7.1.1.1: proton-translocating NAD(P) + transhydrogenase *; EC 7.1.1.2: NADH:ubiquinone reductase (H +-translocating) *; EC 7.1.1.3: ubiquinol oxidase (H ...
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 ...
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, 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 .
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 ...
P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962. Valverde F, Losada M, Serrano A (1997). "Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803". J.