[[5-(3-acetylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [3,4-dihydroxy-5-(6-oxo-3H-purin-9-yl)oxolan-2-yl]methyl hydrogen phosphate
![[[5-(3-acetylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [3,4-dihydroxy-5-(6-oxo-3H-purin-9-yl)oxolan-2-yl]methyl hydrogen phosphate Structure](https://image.chemsrc.com/caspic/016/4002-09-9.png)
[[5-(3-acetylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [3,4-dihydroxy-5-(6-oxo-3H-purin-9-yl)oxolan-2-yl]methyl hydrogen phosphate structure
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Common Name | [[5-(3-acetylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [3,4-dihydroxy-5-(6-oxo-3H-purin-9-yl)oxolan-2-yl]methyl hydrogen phosphate | ||
|---|---|---|---|---|
| CAS Number | 4002-09-9 | Molecular Weight | 664.43000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C22H28N5O15P2+ | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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NAD+ analogs substituted in the purine base as substrates for poly(ADP-ribosyl) transferase.
FEBS Lett. 397 , 17-21, (1996) Poly(ADP-ribosyl) transferase (pADPRT) catalyzes the transfer of the ADP-ribose moiety from NAD+ onto proteins as well as onto protein-bound ADP-ribose. As a result, protein-bound polymers of ADP-ribose are formed. pADPRT itself contains several acceptor site... |
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Interactions of nicotinamide-adenine dinucleotide phosphate analogues and fragments with pigeon liver malic enzyme. Synergistic effect between the nicotinamide and adenine moieties.
Biochem. J. 245 , 407, (1987) The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-mala... |
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Kinetic mechanism of the endogenous lactate dehydrogenase activity of duck epsilon-crystallin.
Arch. Biochem. Biophys. 284 , 285-291, (1991) Initial velocity, product inhibition, and substrate inhibition studies suggest that the endogenous lactate dehydrogenase activity of duck epsilon-crystallin follows an order Bi-Bi sequential mechanism. In the forward reaction (pyruvate reduction), substrate i... |
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Rat liver S-adenosylhomocysteinase. Spectrophotometric study of coenzyme binding.
Biochim. Biophys. Acta 994 , 172-179, (1989) Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel elect... |