• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.2
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• pp.314-319
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• 2001

In the present study, effects of $\beta$-alanine, a known taurine antagonist for its structural similarity, on the adaptive regulation and kinetic behavior of the taurine transporter were investigated in the HT-29, human colon carcinoma cell line. Pretreatment of the cell with $\beta$-alanine(10mM) for varying periods from 3 to 30 hrs significantly reduced the taurine uptake compared to the value for control cells. This decrease in the taurine transporter activity was dependent on the incubation time with $\beta$-alanine, and the maximal down-regulation of the transporter activity was observed in cells pretreated with $\beta$-alanine for 24 hrs (25% of the control value, p<0.01). The taurine transporter appears to bind exclusively with $\beta$-alanine in the HT-29 cells since the same concentration of $\alpha$-alanine added in the culture medium for 24 hrs did not influence the taurine uptake. Kinetic analyses of the taurine transporter activity was performed in the HT-29 cell line with varying taurine concentration (5~60$\mu$M) in the uptake medium. Active taurine uptake was significantly lower in $\beta$-alanine pretreated cells compared to the value for control cells in the range of taurine concentration used in the experiment (p<0.001). The cells pretreated with $\beta$-alanine showed a 50% lower maximal velocity (Vmax, 1.7$\pm$2.0 nmole.mg $protein^{-1}$.$30min^{-1}$), and a 99% higher Michaelis constant (Km, 40.3$\pm$7.6$\mu$M) than the control values (3.3$\pm$1.9 nmole.mg $protein^{-1}$.$30min^{-1}$, and 20.3$\pm$2.1$\mu$M, respectively). These results on kinetic data suggest that $\beta$-alanine induced down-regulation of the taurine transporter activity was associated with decreases in both maximal velocity and affinity of the transporter.

• The Korean Journal of Physiology
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• v.24 no.1
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• pp.171-180
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• 1990

In 19 cats anesthetized with ${\alpha}-chloralose$ effects of taurine and ${\beta}-alanine$ on the responses of wide dynamic range (WDR) cells to mechanical, chemical and thermal stimuli were investigated in the lumbar spinal cord of the cat. Also studied was an interaction of strychnine with taurine in affecting the activities of WDR cells. Following intravenous administration of taurine, the responses of WDR cells to all types of mechanical stimuli were markedly enhanced, demonstrating that the response to pressure was most sensitive to taurine action. When the receptive field was exposed to thermal stimuli ($50^{\circ}C$) for 20 sec. taurine increased activity of WDR cell to 169.5% of the control value. The $K^{+}$-induced activation of WDR cells was invariably suppressed after taurine administration. Intravenously administered strychnine remarkably reduced the enhanced response of WDR cell to natural stimuli resulting from intravenous administration of taurine. Also ${\beta}-alanine$ markedly activated the response of spinal dorsal horn cell to natural mechanical stimuli. These findings suggest that neutral amino acid and its derivative such as ${\beta}-alanine$ and taurine can enhance the response of WDR cells to different stimuli in cats.

• Korean Journal of Microbiology
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• v.54 no.2
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• pp.136-139
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• 2018

The inhibitory compound (Compound S) against Ralstonia solanacearum and its conversion product (Compound S') were isolated from the culture filtrate of Bacillus subtilis JW-1 using a series of chromatography procedures. The structures were elucidated as alanyl-L-${\beta}$-(2,3-epoxycyclohexyl-4-one)alanine and alanyl-L-${\beta}$-(2,3-dihydroxycyclohexyl-4-one)alanine, respectively on the basis of nuclear magnetic resonance spectral data, including $^1H$, $^{13}C$, $^1H-^1H$ correlation spectroscopy and heteronuclear multiple bond correlation spectroscopy. The compound S exhibited a broad antimicrobial activity against $G^+$, $G^-$ bacteria, Saccharomyces cerevisiae and Candida albicans. The activity loss of the conversion product revealed that the epoxy function was essential for activity of Compound S.

• BMB Reports
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• v.32 no.5
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• pp.480-485
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• 1999

Tyrosine phenol-lyase of thermophilic Symbiobacterium sp. SC-1, which is obligately and symbiotically dependent on thermophilic Bacillus sp. SK-1, was purified and characterized. The enzyme is composed of four identical subunits and contains approximately 1 mol of pyridoxal 5'-phosphate (PLP) per mol subunit as a cofactor. The enzyme showed absorption maxima at 330 and 420 nm, and lost this absorption profile by treatment with phenylhydrazine. The apparent dissociation constsnt, $K'_D$, for PLP was determined with the apoenzyme to be about $1.2\;{\mu}M$. The isoelectric point was 4.9. The optimal temperature and pH for the $\alpha,\beta$-elimination of L-tyrosine were found to be $80^{\circ}C$ and pH 8.0, respectively. The substrate specificity of the enzyme was very broad: L-amino acids including L-tyrosine, 3,4-dihydroxyphenyl-L-alanine (L-DOPA), L-cysteine, L-serine, S-methyl-L-cysteine, $\beta$-chloro-L-alanine, and S-(o-nitrophenyl)-L-cysteine all served as substrates. D-Tyrosine and D-serine were also decomposed into pyruvic acid and ammonia at rates of 7% and 31% relative to their corresponding L-enantiomers, respectively. D-Alanine, which was inert as a substrate in a, $\beta$-elimination, was the only D-amino acid racemized by the enzyme. The $K_m$ values for L-tyrosine, L-DOPA, S-(o-nitrophenyl)-L-cysteine, $\beta$-chloro-L-alanine, and S-methyl-L-cysteine were 0.19, 9.9, 0.36, 12, and 5.5 mM, respectively.

• Analytical Science and Technology
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• v.8 no.3
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• pp.359-364
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• 1995

Urinary dipeptidase(Udpase) was assayed by fluorometric analysis of NADH which was produced from an indicator enzyme, L-alanine dehydrogenase. The reaction mixture was consisted of a dipeptide(L-ala-L-ala), ${\beta}-NAD^+$, L-alanine dehydrogenase in 12.5 mM sodium carbonate buffer, pH 9.0, and urinary dipeptidase which initiated the reaction. The fluorescence intensity of NADH was measured as a function of time with the excitation wavelength at 340nm and emission at 460nm. Comparison of this fluorometric method with the conventional spectrophotometric method utilizing glycyldehydrophenylalanine(Gdp) as substrate provided the correlation coefficient of 0.996 and increased the sensitivity more than ten times.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.43 no.1
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• pp.19-22
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• 1998

Effects of acute anoxia on carbohydrate hydrolytic enzyme activities and free amino acid contents in malt were examined. Malts were prepared with barley grains germinated for 7 days which contained the highest levels of amylolytic and(1-3,1-4)-$\beta$-glucanase activities. $\alpha$-Amylase and $\beta$-amylase activities in malts were not significantly affected by anoxia for 5 or 10 h.(1-3,1-4)-$\beta$-Glucanase activity, however, decreased about 7 to 10% by anoxia for 5 or 10 h. Alanine and $\gamma$-aminobutyric acid content changed drastically. Alanine contents in malts increased by 2.2- and 2-fold, and $\gamma$-aminobutyric acid contents by 1.4- and 1.9-fold under anoxia for 5 and 10 h, respectively.

• Toxicological Research
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• v.15 no.1
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• pp.109-115
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• 1999

The antiosidant activity of carnosine and related compounds such as anserine, homo-carnosine, histidine, and $\beta$-alanine which are found in most mammalian tissues, was investigated using hypochlorite (HOCl)-induced oxidant systems. Carnosine and related compounds were protective against HOCl-induced ascorbic acid oxidation, as determined by UV absorbance at 265nm. L-histidine was the most effective among them. The inhibitory effect of these compounds was strongly associated with a decrease in HOCl. It was also found that carnosine and related compounds significantly protected against the HOCl-mediated erythrocyte damage, as determined by hemoglobin release and gemolysis (p<0.05). Carnosine and anserine also inhibited of $\alpha$-antiprotease($\alpha$-AP) by HOCl, thereby inactivating porcine elastase. The inhibitory effect of carnosine on inactivation of $\alpha$-AP by HOCl depended on the concentration of carnosine and on the time preincubated with HOCl. Homocarnosine, histidine, and $\beta$-alanine did not inhibit the reaction. These results indicate that carnosine and related compounds can neutralize or scavenge HOCl. Thus, these compounds may play an important role in protecting against HOCl-mediated damage of biomolecules in vivo.

• Korean Journal of Food Science and Technology
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• v.1 no.1
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• pp.74-77
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• 1969

In this study, three kinds of Korean snake wine (50 V% alcohol extracts) were determined by amino acid analyzer and were discussed as follows. 1. Salmosa Ju and Nungsa Ju were composed of 22 free amino acids: cysteic acid, aspartic acid, threonine, serine, glutamic acid, proline, glycine, alanine, cystine, valine, methionine, iso-leucine, allo-iso-leucine, leucine, nor-leucine, tyrosine, phenylalanine, ${\beta}-alanine$, lysine, arginine, histidine, trytophan. 2. Doksa Ju were composed of 21 free amino acids which were all same as above except missing histidine. 3. The free amino acid composition were almost identical in Doksa Ju, Salmosa Ju and Nungsa Ju quantitatively. 4. The contents of cysteic acid, glutamic acid, glycine, alanine, valine, leucine and lysine were relatively high, on the other hand, methionine, allo-iso-leucine, nor-leucine, and tryptophan were trace amount in every snake wine. 5. Eleven unknowns of ninhydrin positives were identified in the every snake wine. 6. The free amino acids in snake wines were various in kind as compared with in beer, Japanese sake and Korean Tack Ju. Especially cysteic acid, allo-iso-leucine, nor-leucine and ${\beta}-alanine$ in snake wines were missed in every cereal wine.

• Journal of Life Science
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• v.16 no.1
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• pp.44-48
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• 2006

The gene for a L-aspartate $\beta-decarboxylase$ (ADC) from Enterococcus faecalis was cloned and sequenced. The gene comprised an open reading frame of 1,611 base pairs, which encodes a protein of 58,960 Da consisting of 536 amino acid residues. The gene was subcloned into an expression plasmid for overexpression of the ADC. The recombinant ADC was produced using E. coli as the host and purified to homogeneity. Our result showed that the ADC may be obtained from bacteria known nucleotide sequence. Thus, we suggest that high value L-alanine might be produced by low value aspartate.

• Proceedings of the Korean Nutrition Society Conference
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• 2000.11a
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• pp.60-60
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• 2000