P2171
3-Pyridinealdehyde adenine dinucleotide
Synonym(e):
3-Pyridinealdehyde-DPN
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About This Item
Assay
≥90%
Lagertemp.
−20°C
SMILES String
Nc1ncnc2n(cnc12)C3OC(COP(O)(=O)OP(O)(=O)OCC4OC(C(O)C4O)[N]5=CC(C=O)=CC=C5)C(O)C3O
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Anwendung
3-Pyridinealdehyde adenine dinucleotide is an analogue of NAD that may be used to study the structure and function of NAD binding enzymes such as glyceraldehyde 3-phosphate dehydrogenase, NAD malic enzymes, lactate dehydrogenase and saccharopine dehydrogenase from S. cerevisiae.
Verlinkung
Analog of NAD
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Biochemistry, 31(17), 4174-4180 (1992-05-05)
Lactate dehydrogenase catalyzes the stereospecific hydride transfer to and from the re face of the nicotinamide coenzyme. The demonstrated probability of transfer to the si face of less than 2 x 10(-8) indicates that the free energy of any diastereotopic
The Journal of biological chemistry, 250(5), 1734-1740 (1975-03-10)
Glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde-3-phoshate:nicotinamide adenine dinucleotide oxidoreductase (phosphorylating), EC 1.2.1.12) forms a complex with 3-pyridinealdehyde-NAD which survives precipitation with 7% perchloric acid. The molar ratio bound 3-pyridinealdehyde-NAD to the enzyme is 2.5 to 2.9. Lactate, malate, and alcohol dehydrogenases do
Biochemistry, 46(25), 7625-7636 (2007-06-05)
A survey of NADH, alpha-Kg, and lysine analogues has been undertaken in an attempt to define the substrate specificity of saccharopine dehydrogenase and to identify functional groups on all substrates and dinucleotides important for substrate binding. A number of NAD
Biochemistry, 30(23), 5755-5763 (1991-06-11)
Deuterium isotope effects and 13C isotope effects with deuterium- and protium-labeled malate have been obtained for both NAD- and NADP-malic enzymes by using a variety of alternative dinucleotide substrates. With nicotinamide-containing dinucleotides as the oxidizing substrate, the 13C effect decreases
Biochemistry, 23(23), 5479-5488 (1984-11-06)
Since hydride transfer is completely rate limiting for yeast formate dehydrogenase [Blanchard, J.S., & Cleland, W. W. (1980) Biochemistry 19, 3543], the intrinsic isotope effects on this reaction are fully expressed. Primary deuterium, 13C, and 18O isotope effects in formate
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