• Journal of Microbiology
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• 제44권2호
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• pp.243-247
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• 2006

Mycobacterium sp. strain JC1 was capable of growth on benzylamine as a sole source of carbon and energy. The primary deamination of benzylamine was mediated by an inducible amine oxidase, which can also oxidize tyramine, histamine, and dopamine. Inhibitor study identified this enzyme as a copper-containing amine oxidase sensitive to semicarbazide.

• Preventive Nutrition and Food Science
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• 제22권3호
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• pp.211-215
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• 2017

The individual Maillard reactions of glucose, glucosamine, cyclohexylamine, and benzylamine were studied at a fixed temperature of $120^{\circ}C$ under different durations by monitoring the absorbance of the final products at 425 nm. Glucosamine was the most individually reactive compound, whereas the reactions of glucose, cyclohexylamine, and benzylamine were not significantly different from each other. Maillard reactions of reaction mixtures consisting of glucosaminecyclohexylamine, glucosamine-benzylamine, glucose-cyclohexylamine, and glucose-benzylamine were also studied using different concentration ratios under different durations at a fixed temperature of $120^{\circ}C$ and pH 9. Maillard reactions in the pairs involving glucosamine were observed to be more intense than those of the pairs involving glucose. Finally, with respect to the concentration ratios, it was observed that in most instances, optimal activity was realized, when the reaction mixtures were in the ratio of 1:1.

• Bulletin of the Korean Chemical Society
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• 제35권9호
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• pp.2673-2678
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• 2014

The detailed mechanisms of the efficient $\small{L}$-proline and pyrrolidine catalyzed transamidation of acetamide with benzylamine have been investigated using density functional theory (DFT) calculations. Our calculated results show: (1) the mechanisms of two catalytic cycle reactions are similar. However, the rate-determining steps of their reactions are different for the whole catalytic process. One is the intramolecular nucleophilic addition reaction of 1-COM, the other is hydrolysis reaction of 2-C. (2) COOH group of $\small{L}$-proline is essential for efficient transamidation. The computational results are in good agreement with the experiment finding and mechanism resported by Rao et al. for $\small{L}$-proline-catalyzed synthesis of amidesin good to excellent yields.

• Bulletin of the Korean Chemical Society
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• 제11권6호
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• pp.546-552
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• 1990

Enthalpies of solution of aniline, pyridine and benzylamine in iso-dielectric mixtures of methanol with acetonitrile (AN), nitrobenzene (NB) and nitromethane (NM) have been measured calorimetrically. The solute-solvent interaction was analyzed using a model developed by Waghorne et al. and found that the relatively weak base, aniline, tended to behave anomalously, especially in the NB and NM binary systems by forming bidentate hydrogen bonds between the two-$NH_2$ hydrogens and the two-$NO_2$ oxygens. Pyridine and benzylamine were found to be preferentially solvated by methanol in all the binary mixtures.

• Bulletin of the Korean Chemical Society
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• 제12권3호
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• pp.282-286
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• 1991

Kinetic studies of the reactions of benzyl benzenesulfonates with benzylamines in methanol and acetonitrile have been carried out. The reaction was found to proceed by a dissociative $S_N2$ in MeCN but by an associative $S_N2$ mechanism in MeOH. The transition state was rather loose in MeCN whereas it was tight in MeOH, in contrast to a tighter TS in MeCN for the corresponding reactions with aniline. The reaction of benzylamine in MeOH was characteristic of the highly solvated nucleophile, benzylamine, compared to the normal reaction in MeCN.

• Bulletin of the Korean Chemical Society
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• 제20권9호
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• pp.1017-1020
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• 1999

The aminolysis reactions of thiophenyl phenylacetates with benzylamines are investigated in acetonitrile at 55.0℃. Relatively large selectivity parameters, βx≒ 1.5, βz = -1.5~-1.8 and βxz = 0.92 together with the valid reactivity-selectivity principle are consistent with stepwise acyl transfer mechanism with rate limiting expulsion of the leaving group, thiophenolate anion, from the tetrahedral intermediate, T ± . The first order kinetics with respect to the benzylamine concentration and the realtively large secondary kinetic isotope effect (kH / kD = 1.2-1.7) involving deuterated benzylamine nucleophiles suggest a four center type transition state in which concurrent leaving group departure and proton transfer are involved.

• Bulletin of the Korean Chemical Society
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• 제19권11호
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• pp.1198-1202
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• 1998

Aminolysis of aryl thiol-2-furoates and thiol-2-thiophenates with benzylainines are investigated in acetonitrile at 50.0 ℃. Relatively large selectivity parameters, ρx(βx), ρz(βx) and ρxz (> 0) together with the valid reactivity-selectivity principle are consistent with a stepwise acyl transfer mechanism with rate-limiting expulsion of the leaving group, thiophenolate anion, from the tetrahedral intermediate, T±. The first-order kinetics with respect to the benzylamine concentration and the relatively large secondary kinetic isotope effect involving deuterated benzylamine nucleophiles suggest a four-center type transition state in which concurrent leaving group departure and proton transfer are involved.

• 대한화학회지
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• 제44권5호
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• pp.442-447
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• 2000

$\alpha$-Functionalized benzylamine(Nu=OAc, OMe, $N_3$)은 유기합성의 출발물질 또는 synthon으로서 매우 유용할 것이다. 본 연구에서는 benzylphthalimide를 137$^{\circ}C$, chlorobenzene 용매 하에서 NBS/NaOAc/HOAc조건을 사용하여, 높은 수율로 phthalimide-benzyl acetate을 얻는 방법을 개발하였다. 마지막으로, phthalimide-benzyl acetate을 $NH_2NH_2$/HOAc 조건 하에서, amino(phenyl)methyl acetate (1)을 합성하였다.

• Bulletin of the Korean Chemical Society
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• 제19권8호
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• pp.891-893
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• 1998

• Archives of Pharmacal Research
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• 제11권3호
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• pp.213-217
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• 1988

The effects of ethanol and acetaldehyde on monoamine oxidase activity in mouse liver mitochondrial fraction were studied. In vivo, a single dose of ethanol increased the hepatic monoamine oxidase activity compared to control group, and chronic ethanol consumption also increased the enzyme activity using tyramine, benzylamine or serotonin as substrate. Acetaldehyde, the metabolite of ethanol, significantly increased monoamine oxidase activity more than ethanol did. In contrast to the in vivo results, it was found that the monoamine oxidase activity was inhibited in vitro by ethanol or acetaldehyde in the dose-dependent manner.