Ethanol as substrate

Class 1 or 2, depending on the substrate used. We can see from Table 2, for example, that sucdnoglycan biosynthesis leads to a net production of ATP (Class 2) with ethanol as substrate, but the biosynthesis is energy requiring (Class 1) with glucose as substrate. 

Horse Uver alcohol dehydrogenase Inhibited by aliphatic, cychc and aromatic oximes using ethanol as substrate 123... 

High reactivity was observed for 21b, and 21a was found to be the most selective. In the presence of 10 mol% 21a selectivity factors as high as 6.5 were observed with racemic 1-(1-naphthyl)ethanol as substrate (Scheme 12.6) [18]. The TBS analog of 21a was found to be good catalyst for asymmetric addition of methanol to a variety of prochiral aryl alkyl ketenes [18]. The catalytic asymmetric addition of achiral alcohols to prochiral ketenes is discussed in Section 13.2. 

Brookhart and co-workers found that the cationic a-silane complex [CpFe(CO)(PR3)(HSiEt3)]+ was observable by NMR at RT but only in the presence of excess silane (sacrificial removal of trace H20 as Et3SiOH) and could not be isolated as a solid (122). The [CpFe(CO)(PR3)] fragment catalyzed silane alcoholysis in the presence of the BArF counterion (123). Although rapid deactivation of the catalyst occurred with ethanol as substrate, phenol reacted continuously with turnover numbers up to 80 min-1. It was proposed (Scheme 9)... 

In incubations of each isoenzyme with linoleic acid dispersed in ethanol as substrate. Solutions were gassed with oxygen at 0°C. Calcium ion was either present (0.55mM) or absent. 

Isozymes containing the atypical subunit have a pH optimum around pH 8.5-8.S with ethanol as substrate, whereas the other isozymes have an optimum at pH 10.8-11.5 (72,76), agreeing with the properties of the atypical enzyme in the liver (64,65). The small structural difference, resulting from the mutant allele at the ADH2 locus, thus contributes a considerable effect on the enzymic activity. 

On the other hand, Shore and Gutfreund 298) found evidence in their transient kinetic studies of LADH using ethanol as substrate that the two subunits are equivalent. Some possible causes for the different results obtained by the two groups have been discussed 359). 

Scheme 39 Proposed mechanism for H2 generation with ethanol as substrate.

Fig. 2. The effect of unsaturated fatty acid depletion on mitochondrial P/O ratios measured in vitro. Cells of strain KDl 15 were grown in a glucose-limited chemostat at various levels of unsaturated fatty acid, and the mitochondria were isolated. Mitochondrial P/O ratios were determined as described by Haslam, with either succinate (A) or ethanol ( ) as substrate.

As solvent an alcohol—often ethanol—as well as water or acetic acid can be used. The reaction conditions vary with the substrate various CH-acidic compounds can be employed as starting materials. The Mannich bases formed in the reaction often crystallize from the reaction mixture, or can be isolated by extraction with aqueous hydrochloric acid. 

Saccharomyces cerevisiae is anaerobically grown in a continuous culture at 30°C. Glucose is used as substrate and ammonia as nitrogen source. A mixture of glycerol and ethanol is produced. At steady-state condition mass the flow rate is stated. The following reaction is proposed for the related bioprocess 4,6... 

The special salt effect is a constant feature of the activation of substrates in cages subsequent to ET from electron-reservoir complexes. In the present case, the salt effect inhibits the C-H activation process [59], but in other cases, the result of the special effect can be favorable. For instance, when the reduction of a substrate is expected, one wishes to avoid the cage reaction with the sandwich. An example is the reduction of alkynes and of aldehydes or ketones [60], These reductions follow a pathway which is comparable to the one observed in the reaction with 02. In the absence of Na + PFg, coupling of the substrate with the sandwich is observed. Thus one equiv. Na+PFg is used to avoid this cage coupling and, in the presence of ethanol as a proton donor, hydrogenation is obtained (Scheme VII). 

With endogeneous pectic polysaccharides as substrates, the pectin methyhransferase activity was measured as radioactivity linked to oxalate-soluble polys x harides after extensive washing of microsomes with IM ethanolic NaCL Figure 2 shows that the rate of methylesterification of pectic substances was maximal on days 4 and 6 these maximum activities were observed within this period in at least five independent ejqjeriments. On the other hand, little activity was noted in young cells before day 2, and in old cells after day 9. In other words during the stationary phase the newly synthesised pectins remained unesterified because of the lack of pectin methyltransferase activity. 

Another method is based on the same principle,112 in which the [14C]labelled methyl ester of D-galacturonan is prepared by esterification of pectic acid with [,4C]diazomethane. In the course of the enzymic de-esterification, aliquots are removed, and the unreacted substrate is precipitated with acidified ethanol or 1-propanol. After centrifugation, the labelled methanol in the supernatant liquor is determined in a liquid scintillation counter. An advantage of this method lies in the possibility of using, as substrates, short-chain oligo-D-galactosiduronates partially esterified with [14C]methanol. These substrates, beginning with the trisaccharide, are not soluble in 1 4 80% phenol-diethyl ether, which is used for the extraction of enzymically released, labelled methanol. 

Ethanol is both an inducer and substrate of CYP2E1. Indeed, CYP2E1 seems to be structurally geared to favor small volatile molecules such as ketones, aldehydes, alcohols, halogenated alkenes, and alkanes as substrates (36). Moreover, many of these same compounds, like ethanol, are inducers of the enzyme. A major mechanism by which this diverse group of compounds appears to initiate induction is by inhibiting normal enzyme degradation. 

The ALDs are a subset of the superfamily of medium-chain dehydrogenases/reductases (MDR). They are widely distributed, cytosolic, zinc-containing enzymes that utilize the pyridine nucleotide [NAD(P)+] as the catalytic cofactor to reversibly catalyze the oxidation of alcohols to aldehydes in a variety of substrates. Both endobiotic and xenobiotic alcohols can serve as substrates. Examples include (72) ethanol, retinol, other aliphatic alcohols, lipid peroxidation products, and hydroxysteroids (73). 

The homogeneous solvolysis of this substrate in aqueous ethanolic solvents can be monitored by the change in conductance as HCl is produced. Initial studies of the reaction in aqueous ethanol as solvent at 25 °C using a cleaning bath (45 kHz) revealed modest rate enhancements (up to about 2-fold) with the larger values being obtained in the more alcoholic media [37]. Similar results were found for the solvo-lyses in aqueous propan-2-ol and 2-methylpropan-2-ol. More substantial rate enhancements were obtained in the more ethanolic media and at lower temperature [38,39]. Detailed studies of the aqueous ethanol system led to the following main conclusions ... 

Tincture of the dried seed, on agar plate at a concentration of 30 p,L/disc, was inactive on Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Extract of 10 g plant material in 100 mL ethanol was used b Anticoagulation activity. Serpin BSZx (an inhibitor of trypsin and chemotrypsin) inhibited thrombin, plasma kallikrein, factor Vlla/tissue factor, and factor Xa at heparin-independent association rates. Only factor Xa turned a significant fraction of BSZx over as substrate. Activated protein C and leukocyte elastase were slowly inhibited by BSZx, whereas factor Xlla, urokinase and tissue type plasminogen activator, plasmin and pancreas kallikrein, and elastase were not or only weakly affected. Trypsin from Fusarium was not inhibited, while interaction with subtilisin Carlsberg and Novo was rapid, but most BSZx was cleaved as a substrate L... 

In this work we extend our study to the hydrogenation and isomerization of a series of a,p-unsaturated alcohols, such as 2-propen-l-ol (A2), (E -2-buten-l-ol (EB2), (" -2-penten-l-ol (ZP2), (E -2-penten-l-ol (EP2), (" -2-hexen-l-ol (ZH2), (E -2-hexen-l-ol (EH2), carried out in the presence of RhCl(PPh3)3, with and without triethylamine (NEts), at 303 K, using ethanol as solvent. The major targets of our research are to investigate the influence of the unsaturated alcohol structure on the product distribution and to verify the possibility of extending the results, previously obtained with (" -2-butene-1,4-diol, to other analogous substrates. 

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