Nicotinaldehyde
Nicotinaldehyde structure
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Common Name | Nicotinaldehyde | ||
|---|---|---|---|---|
| CAS Number | 500-22-1 | Molecular Weight | 107.110 | |
| Density | 1.1±0.1 g/cm3 | Boiling Point | 209.9±0.0 °C at 760 mmHg | |
| Molecular Formula | C6H5NO | Melting Point | 8°C | |
| MSDS | Chinese USA | Flash Point | 60.0±0.0 °C | |
| Symbol |
GHS02, GHS05, GHS07 |
Signal Word | Danger | |
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[Selenazoles. X. [1]. Beta-methyl-beta-4-R-selenazolyl-2)-hydrazones of acetaldehyde, benzaldehyde, isonicotinaldehyde, nicotinaldehyde and picolinaldehyde].
Ann. Univ. Mariae Curie. Sklodowska. Med. 39 , 33-40, (1984)
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[Selenazoles. IX. [9]. 3-methyl-4-R-selenazolidene-2-hydrazones of acetaldehyde, benzaldehyde, isonicotinaldehyde, nicotinaldehyde and picolinaldehyde].
Ann. Univ. Mariae Curie. Sklodowska. Med. 39 , 25-31, (1984)
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Kinetic mechanism of sheep liver NADPH-dependent aldehyde reductase.
Biochem. J. 242(1) , 143-50, (1987) The kinetic mechanism of the major sheep liver aldehyde reductase (ALR1) was studied with three aldehyde substrates: p-nitrobenzaldehyde, pyridine-3-aldehyde and D-glucuronate. In each case the enzyme mechanism was sequential and product-inhibition studies we... |
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Subcellular localization of aldehyde reductase activities in ox brain.
Biochem. J. 197(3) , 715-20, (1981) The distribution of the two principal isoenzymes of aldehyde reductase (EC 1.1.1.2) has been studied in ox brain. The more active of these, which has been termed the high-Km enzyme, has been shown to be located in the cytosol and the less abundant low-Km form... |
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Effect of ozone on nicotine desorption from model surfaces: evidence for heterogeneous chemistry.
Environ. Sci. Technol. 40(6) , 1799-805, (2006) Assessment of secondhand tobacco smoke exposure using nicotine as a tracer or biomarker is affected by sorption of the alkaloid to indoor surfaces and by its long-term re-emission into the gas phase. However, surface chemical interactions of nicotine have not... |
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Kinetic studies with the low-Km aldehyde reductase from ox brain.
Biochem. J. 227(2) , 621-7, (1985) Initial-rate studies of the low-Km aldehyde reductase-catalysed reduction of pyridine-3-aldehyde by NADPH gave families of parallel double-reciprocal plots, consistent with a double-displacement mechanism being obeyed. Studies on the variation of the initial ... |
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Synthesis of multisubstituted quinolines from Baylis-Hillman adducts obtained from substituted 2-chloronicotinaldehydes and their antimicrobial activity.
Bioorg. Med. Chem. 14(13) , 4600-9, (2006) Baylis-Hillman acetates were synthesized from substituted 2-chloronicotinaldehydes and were conveniently transformed into multisubstituted quinolines and cyclopenta[g]quinolines on reaction with nitroethane or ethyl cyanoacetate via a successive S(N)2'-S(N)Ar... |
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The kinetics and mechanism of pig-liver aldehyde reductase. Comparative studies with pyridine-3-aldehyde and p-carboxybenzaldehyde.
Eur. J. Biochem. 131(2) , 375-81, (1983) Initial-rate measurements were made of the reduction of pyridine-3-aldehyde and p-carboxybenzaldehyde by NADPH catalyzed by pig liver aldehyde reductase I. The initial velocity analysis and product inhibition data suggest that aldehyde reductase I obeys a com... |
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Anti-malarial activity of Baylis-Hillman adducts from substituted 2-chloronicotinaldehydes.
Bioorg. Med. Chem. Lett. 15(24) , 5378-81, (2005) New Baylis-Hillman adducts are synthesized based on substituted 2-chloronicotinaldehydes and screened for their in vitro anti-malarial activity against chloroquine sensitive and chloroquine resistant Plasmodium falciparum. Out of the six new compounds synthes... |
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Characterization of nicotinamidases: steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism.
Biochemistry 49(49) , 10421-39, (2010) Nicotinamidases are metabolic enzymes that hydrolyze nicotinamide to nicotinic acid. These enzymes are widely distributed across biology, with examples found encoded in the genomes of Mycobacteria, Archaea, Eubacteria, Protozoa, yeast, and invertebrates, but ... |