P2171
3-Pyridinealdehyde adenine dinucleotide
Synonim(y):
3-Pyridinealdehyde-DPN
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About This Item
Wzór empiryczny (zapis Hilla):
C21H26N6O14P2
Numer CAS:
Masa cząsteczkowa:
648.41
Numer MDL:
Kod UNSPSC:
41106305
Identyfikator substancji w PubChem:
Próba
≥90%
temp. przechowywania
−20°C
ciąg SMILES
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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Zastosowanie
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.
Powiązanie
Analog of NAD
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
R D LaReau et al.
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
E J Hill et al.
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
Hengyu Xu et al.
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
Sahng Ha Lee et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 18(18), 5490-5495 (2012-04-11)
NAD analogues can be employed as artificial electron carriers for photoenzymatic synthesis under visible light. Four different NAD analogues that have a 3-substituted pyridine ring have been investigated. 3-Acetylpyridine adenine dinucleotide and 3-pyridinealdehyde adenine dinucleotide were photochemically reduced much more
J D Hermes et al.
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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