• Journal of Microbiology and Biotechnology
• /
• v.7 no.5
• /
• pp.329-332
• /
• 1997

Cell-free extracts of Streptomyces neyagawaensis SL-387 grown on a chemically defined medium supplemented with DL-3-amino-3-phenylpropionic acid (APP) produced N-acetyl-APP (Ac-APP) in the presence of APP and acetyl coenzyme A. The APP obtained by acid hydrolysis of the Ac-APP was D-configuration: $[\alpha]_D+6.5^{\circ}(H_2O)\;at\;20^{\circ}C$, optical purity 92% enantiomeric excesses (ee). These results suggest that an N-acetyltransferase exists in the cell-free extract as a novel enzyme with specificity for D-APP.

• Journal of the Korean Chemical Society
• /
• v.54 no.6
• /
• pp.680-686
• /
• 2010

Inhibition effects of alanine(Ala), asparagine(Asn), aspartic acid(Asp), glutamine(Gln) and methionine(Met) on the corrosion of copper were investigated in aerated artificial sea water. Amino acid adsorption process in copper surface can be explained by Temkin logarithmic isotherm due to the interaction between the adsorbed molecules. The inhibition efficiency for the copper corrosion depended on the concentration of amino acids.

• Korean Journal of Weed Science
• /
• v.10 no.3
• /
• pp.227-232
• /
• 1990

The effects of alachlor [2-chloro-2', 6' diethyl-N-(methoxymethyl) acetanilide] treatment on nucleic acid, amino acid and protein synthesis were studied. The amide herbicide alachlor blocks the biosynthesis of the amino acids isoleucine, valine and aromatic amino acid in oat root tips. Nucleic acid was inhibited, but was not proportional to reduction in protein synthesis. $1{\times}10^{-4}M$ of alachlor treatment of oat roots inhibited 36% DNA synthesis, but DNA synthesis was not inhibited at $1{\times}10^{-5}M$. RNA synthesis was inhibited by $1{\times}10^{-5}M$ and $1{\times}10^{-4}M$ of alachlor 16 and 27%, respectively, while inhibition of protein synthesis did occur at same concentrations. Inhibition of protein synthesis also did not occur at concentration below $1{\times}10^{-4}M$ alachlor. It suggest that inhibition of protein sythesis caused significantly by alachlor($1{\times}l0^{-3}M$) result from secondary action.

• The Korea Journal of Herbology
• /
• v.22 no.2
• /
• pp.51-63
• /
• 2007

Objectives : For the congenital feeble, the Gongjindan is useful medicine. The experiment is to estimate the value of the Gongjindan as therapeutic agent preventing against aging with an analysis of the ingredients and the bio-activating effects by enzymologic methods. Methods : General ingredients' of the Gongjindan's extract were analyzed first and the quantitative analysis of a reducing sugar, a soluble protein, an amino acid and minerals was made. The Gongjindan, which is extracted, concentrated, and freeze drying with water, ethanol and chloroform, have got applied for the experiment. The effects on electronic donating ability, SOD-like activity, nitric oxide inhibition, xanthine oxidase inhibition, whitening effect have been investigated in the physiological activity measurement of function experiment. Results : The contained amino acid, in order of high amount, is Arginine, Alanine, Glutamic acid, Proline and the contained free amino acid is Glutamic acid, Leucine, Lysine, Phenylalanine. The derivative of free amino acid is ${\gamma}-Aminoisobutyric$ acid, Phosphoserine, Taurine. And the Gongjindan is containing 13 species of minerals in order of Ca>K>Na>Mg>Fe>AI>Mn. Then, to assure of the Gongjindan's capability of anti-oxidation, these following subjects-polyphenol, electronic donating ability, SOD-like activity, nitric oxide inhibition, xanthine oxidase inhibition, tyrosinase inhibition- are analyzed and show high activity especially the most in ethanol extracts. Conclusion : With this analysis of ingredients, the Gongjindan is containing many materials functioning as anti-oxidation, anti-aging, anti-fatigue, neurotransmitter and immune agent. Moreover, In every water, ethanol, chloroform extracts, the Gongjindan's capability of anti-oxidation is confirmed so that we can apply to patients' treatment clinically.

• Journal of the Korean Chemical Society
• /
• v.5 no.1
• /
• pp.38-41
• /
• 1961

By varying groups on biologically active molecules, it is possible to produce analogues which sometimes inhibit the action of the parent compound. Such is true of taurine(${\beta}$-amino-ethane sulfonic acid)as an analogue of ${\beta}$-alanine and of pantoyl taurine for pantothenic acid. It seemed possible that the sulfonic acid analogues of amino acids built into peptides might possibly produce inhibition of the parent peptide. Tauryl-L-histidine was selected to prepare as an analogue of carnosine(${\beta}$-alanyl-L-histidine). There were several reasons for this choice. Camosine causes a slight contraction of isolated uterine muscle and inhibition of this action can be easily tested. Also, taurine, being a ${\beta}$-amino sulfonic acid, is much more stable than the ${\beta}$-amino sulfonic acids. Phthalyl tauryl-L-histidine methyl ester was prepared by condensing phthalyl tauryl chloride with histidine methyl ester in chloroform. The yields were quite low possibly due to reaction between the acid chloride and the imidazole of histidine. Approximately 50 per cent yield of crude amorphous product was obtained, but upon purification by crystallization they yielded only 25 percent of a pure product. The methyl ester was removed by acid hydrolysis to prevent partial cleavage of the phthalyl group. Crystalline tauryl histidine was then obtained from this acid by removal of the phthalyl group by hydrazinolysis. Tests for inhibition were carried out by comparing the action of camosine on isolated uterine muscle before and after tauryl histidine had been added to the bath surrounding the muscle strip. Only in very high relative concentrations of tauryl histidine was there any demonstrable inhibition.

• Asian-Australasian Journal of Animal Sciences
• /
• v.9 no.1
• /
• pp.45-49
• /
• 1996

A series of in vitro experiments was conducted to investigate response of rumen bacterial deamination to the ionophore salinomycin. Addition of salinomycin to the inoculum, strained rumen fluid, depressed ammonia production from casein, while increased accumulation of ${\alpha}$-amino acids. This suggests an inhibitory effect of salinomycin on ruminal deamination. When the effect in washed bacterial suspension was monitored with individual amino acid, aspartic acid degradation was markedly inhibited by salinomycin. This inhibition was not observed when the mixed rumen bacteria were ultrasonically disrupted and used as the enzyme source. Extent of the inhibition tended to be higher in the bacteria source from sheep on a high roughage diet. From these results it was speculated that the inhibition of deamination with salinomycin is caused by a decreased transport of amino acid into the bacterial cells as well as a decreased proportion of deaminating bacteria in the rumen.

• BMB Reports
• /
• v.34 no.4
• /
• pp.299-304
• /
• 2001

The 3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme of aromatic amino acid-, folic acid-, and phenazine-1-carboxylic acid biosynthetic pathways. DAHP synthase of Bacillus sp. B-6 that produces phenazine-1-carboxylic acid was feedback inhibited by two intermediary metabolites of aromatic amino acid biosynthetic pathways, prephenate and chorismate, but not by other metabolites, such as anthranilic acid, shikimic acid, p-aminobenzoic acid, and 3-hydroxyanthranilic acid. DAHP synthase of Bacillus sp. B-6 was not inhibited by end products, such as aromatic amino acids, folic acid, and phenazine-1-carboxylic acid. The inhibition of DAHP synthase by prephenate and chorismate was non-competitive with respect to erythrose 4-phosphate and phosphoenolpyruvate. Prephenate and chorismate inhibited 50% of the DAHP synthase activity at concentrations of $2{\times}10^{-5}\;M$ and $1.2{\times}10^{-4}\;M$, respectively The synthesis of DAHP synthase of Bacillus sp. B-6 was not repressed by exogenous aromatic amino acids, folic acid, and phenazine 1-carboxylic acid, single or in combinations.

• YAKHAK HOEJI
• /
• v.44 no.3
• /
• pp.279-282
• /
• 2000

The inhibition mode of S-hydroxy-2-phenylalanylaminomethyl-4-pyron ($IC_{50}=24.6{\;}{\mu}M$) on mushroom tyrosinase was investigated using L-tyrosine as a substrate. This inhibitor is the kojic acid derivative, where the C-7 hydroxyl of kojic acid was replaced by amino group and coupled to the carboxyl of L-phenylalanine. The kinetic data obtained show a competitive inhibition pattern.

• Journal of the Korean Chemical Society
• /
• v.63 no.5
• /
• pp.327-334
• /
• 2019

Inhibition effects of cysteine(Cys), methionine(Met), and histidine(His) on the corrosion of cobalt were investigated in deaerated 0.5 M HCl and 0.5 M $H_2SO_4$ solution. All the inhibition efficiency (IE) in the amino acids for the cobalt corrosion depended on the mixed inhibition. However, IE in the solution of $H_2SO_4$ depended more on the anodic and in the solution of HCl on the cathodic inhibition. Amino acid adsorption process on cobalt surface in the solution can be explained by modified Langmuir isotherm. The molecules of histidine dissolved in both of the solution were physically adsorbed due to the electrostatic interaction between the surface of {$Co-Cl^{-{\delta}}$} and the {$-NH_3{^+}$} or {$-NH^+=$} of His. However the other cases of adsorption in this investigation can be explained by chemical adsorption between the empty d-orbital of Co and the lone pair of electron in S-atom in Cys and Met.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.32 no.5
• /
• pp.758-763
• /
• 2003

Amino acid transporters play an important role in supplying nutrients to normal and cancer cells for cell proliferation. System L is a major transport system responsible for the N $a^{＋}$-independent, large neutral amino acids including several essential amino acids. L-type amino acid transporter 1 (LAT1), an isoform of system L amino acid transporter, is highly expressed presumably to support their continuous growth and proliferation in malignant tumors. 2-Aminobicyclo- (2,2,1) -heptane-2-carboxylic acid (BCH) is a model compound for study of amino acid transporter as a system L selective inhibitor. In the present study, we examined whether BCH induced growth inhibition in KB human oral squamous carcinoma cell line or not. The uptake of L-［$^{14}$ C］leucine by KB cells is inhibited by BCH in a concentration dependent manner with a Ι $C_{50}$ value of 75.3$\pm$6.2 ${\mu}{\textrm}{m}$ and a $K_{i}$ value of 98.7$\pm$ 4.1 ${\mu}{\textrm}{m}$. The growth of KB cells is inhibited by BCH in time dependent manner and concentration dependent manner with a Ι $C_{50}$ value of 11.1 $\pm$0.8 mM. In the DNA of KB cells treated with the various concentrations and various periods of BCH, the characteristic ladders associated with DNA fragmentation were not observed. These results suggest that BCH inhibits the growth of KB oral epidermoid carcinoma cells through the inhibition of transport of neutral amino acids into cells without DNA break down. This phenomenon will be a new rationale for anti-cancer therapy.y.