Disease relevance of NSC 6739

• Exposure of lambda phage to triplet acetone, generated via the oxidation of isobutanal by peroxidase, leads to genome lesions [1].
• Specific anosmia for this dialdehyde has precedence in anosmia for various monoaldehydes, most notably isobutyraldehyde [2].

High impact information on NSC 6739

• Elementary reactions have been studied quantitatively in the complex overall process catalyzed by horseradish peroxidase whereby isobutyraldehyde and molecular oxygen react to form triplet state acetone and formic acid [3].
• Transient state kinetics of the reactions of isobutyraldehyde with compounds I and II of horseradish peroxidase [3].
• Enzyme-generated electronically excited carbonyl compounds, Acetone phosphorescence during the peroxidase-catalyzed aerobic oxidation of isobutanal [4].
• The resulting alpha,beta-unsaturated lactam could be condensed with isobutyraldehyde to produce Z-pulchellalactam or converted into siloxypyrrole, which was subjected to the BF(3) x Et(2)O-promoted coupling reaction with isobutyraldehyde to afford E-pulchellalactam after E1-cB elimination and TFA deprotection [5].
• Peroxynitrite is shown here to promote the aerobic oxidation of isobutanal (IBAL) and 3-methyl-2,4-pentanedione (MP) in a pH 7.2 phosphate buffer into acetone plus formate and biacetyl plus acetate, respectively [6].

Biological context of NSC 6739

• Isobutyraldehyde administered by inhalation (whole body exposure) for up to thirteen weeks or two years was a respiratory tract toxicant but was not carcinogenic in F344/N rats and B6C3F1 mice [7].
• Likewise, energy transfer to COL from triplet acetone produced by either isobutanal/horseradish peroxidase system or tetramethyldioxetane thermolysis failed to provoke photoreaction of COL [8].
• A study of the effects of deglycosylation of horseradish peroxidase on protein conformation, as well as on its catalytic activity of oxidation of isobutyraldehyde or its enol form to triplet acetone and formic acid, was performed [9].
• DNA damage during the peroxidase-catalyzed aerobic oxidation of isobutanal [10].

Anatomical context of NSC 6739

• The addition of a precursor of the enol form of isobutanal to neutrophils results in formation of triplet acetone, as attested to by emission from appropriate acceptors and cell damage (Nascimento et al., 1986 Biochim. Biophys. Acta 888, 337-342) [11].

Associations of NSC 6739 with other chemical compounds

• The rates of oxygen uptake and light emission observed when horseradish peroxidase oxidizes isobutyraldehyde or the trimethylsilyl enol ether form of the latter are reduced when the enzyme is 70% deglycosylated [9].
• Acrolein, formaldehyde, and HCl had little effect on any of the surface properties measured whereas isobutyraldehyde and liquid smoke altered the y-A curve but did not increase ymin [12].
• Soybean lipoxygenase shows a secondary peroxidase/oxidase activity: The aerobic reaction with isobutanal, enhanced by hydrogen peroxide as a cosubstrate, yields acetone, exhibits chemiluminescence and consumes oxygen (phi cl = 1.3 x 10(-9) photons/O2 molecule consumed) [13].
• Acetaldehyde and 2-methyl-propanal were also produced on MEA and barley, while 2-pentanone, methyl acetate, 2-butanol and 3-methyl-3-buten-1-ol were observed on soybeans [14].
• A pH of 5.2 apparently inhibited the isobutyl alcohol degradation and lowered the isobutyraldehyde degradation rate, although adaptation of the microorganisms to low pH seemed to occur in the biofilters [15].

References