• Title/Summary/Keyword: carboxylic amino acids

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Regulation of 3-Deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) Synthase of Bacillus sp. B-6 Producing Phenazine-1-carboxylic acid

  • Kim, Kyoung-Ja
    • BMB Reports
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    • v.34 no.4
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    • pp.299-304
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    • 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.

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Chemical Modification of the $\beta$-D-Xylosidase from Bacillus stearothermophilus (화학적 수식에 의한 Bacillus stearothermophilus $\beta$-D-Xylosidase 의 연구)

  • 서정한;최용진
    • Microbiology and Biotechnology Letters
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    • v.22 no.6
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    • pp.636-642
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    • 1994
  • Essential amino acids involving in the catalytic mechanism of the $\beta$-D-xylosidase of Bacillus stearothermophilus were determined by chemical modification studies. Among various che- mical modifiers tested N-bromosuccinimide (NBS), $\rho$-hydroxymercurybenzoate (PHMB), N-ethylma- leimide, 1-[3-(di-ethylamino)-propyl]$-3-ethylcarbodi-imide (EDC), and Woodward's Reagent K(WRK)inactivated the enzyme, resulting in the residual activity of less than 20%. WRK reduced the enzyme activity by modifying carboxylic amino acids, and the inactivation reacion proceeded in the form of pseudo-first-order kinetics. The double-lagarithmic plot of the observed pseudo-first- order rate constant against the modifier concentration yielded a reaction order of 2, indicating that two carboxylic amino acids were essential for the enzyme activity. The $\beta$-D-xylosidase was also inactivated by N-ethylmaleimide which specifically modified a cysteine residue with a reaction order of 1, implying that one cysteine residue was important for the enzyme activity. Xylobiose protected the enzyme against inactivation by WRK and N-ethylmaleimide, revealing that carboxylic amino acids and a cysteine residue were present at the substrate-binding site of the enzyme molecule.

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Competitive Inhibition of Pepsin by Carboxylic Acids (脂肪酸에 依한 Pepsin의 競走的 억제)

  • Hong Dae Shin
    • Journal of the Korean Chemical Society
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    • v.14 no.2
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    • pp.161-168
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    • 1970
  • In order to obtain the more effective evidence, supporting the hypothesis which have been previously described by former report that pepsin (EC 3.4. 4.1) forms a hydrophobic bond with the nonpolar side chain of its substrate, the inhibitory effect of carboxylic acids(from formic acid to iso-butyric acid) on the activity of pepsin to the synthetic dipeptide, N-Carbobenzoxy-L-glutamyl-L-tyrosine, was discussed. The kinetic study showed that the inhibition by carboxylic acids was competitive. The Kidecreased with increasing size of the inhibitor molecule. The $-{\Delta}F^{\circ}$increased linearly with increasing number of carbon atoms in the hydrocarbon chain of the inhibitor. It was confirmed that the hydrophobic bond between more than one side chain of amino acid residues(phenylalanine) in the binding region of the active center of pepsin and the side chain of amino acid residues in the substrate was formed as the first step of its enzymic mechanism. The inhibitory effect of carboxylic acids was due to the competition of the hydrocarbon group of the carboxylic acids with the side chain of the substrate for the hydrophobic binding site(the side chain of phenylalanine) of the pepsin.

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Roles of the Conserved Carboxylic Residues in the Active-Site of 5'-3' Exonuclease of Taq DNA Polymerase

  • Kim, Young-Soo;Shin, Joong-Chul
    • Journal of Microbiology and Biotechnology
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    • v.9 no.4
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    • pp.381-385
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    • 1999
  • Taq DNA polymerase from Thermus aquaticus has been shown to be very useful in a polymerase chain reaction. Taq DNA polymerase has a domain at the amino terminus (residues 1 to 290) that has 5'-3' exonuclease activity and a domain at the C-terminus that catalyzes the polymerase reaction. Taq DNA polymerase is classified into the Pol I family, which is represented by E. coli DNA polymerase I. The alignment of amino acid sequences for the 5'-3' exonuclease domains of the Pol I family DNA polymerases shows ten highly conserved carboxylic amino acids. Crystallographic studies suggested that six of the carboxylic amino acids are clustered within a 7 $\AA$ radius by chelating three metal ions in the active site. Those six carboxylic residues are mutagenized to alanines in order to better understand their function. All six carboxylic residues, Asp l8, Glu1l7, Asp1l9, Asp120, Asp142, and Aspl44, are crucial for catalysis of 5'-3' exonuclease.

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Cyclic Oligopyrroles as Sensors for Absolute Configuration Determination of Carboxylic Acids

  • Lintuluoto Juha M.;Nakayama Kana;Setsune Jun-Ichiro
    • Proceedings of the Polymer Society of Korea Conference
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    • 2006.10a
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    • pp.241-241
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    • 2006
  • Absolute configuration of carboxylic acids, including amino acids can be determined by circular dichroism (CD) exciton chirality method. This method employs cyclic oligopyrroles able to form stable complexes with carboxylic acids. Addition of carboxylic acids to the oligopyrroles induce CD spectrum at the macrocycle absorption region and in which the sign of the $1^{st}$ Cotton effect is determined solely by the absolute configuration of the carboxylic acid. The basicity of the pyrrole nitrogen can be controlled by macrocycle substitution thus yielding more sensitive chirality sensors.

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Syntheses and Central Nervous Depressant Activity of Piperine Derivatives(III) N-Piperoyl Amino Acids (Piperine유도체의 합성 및 중추억제작용에 관한 연구(III) N-Piperoylamino Acid 유도체)

  • 이한구;임중기;이은방;우원식
    • YAKHAK HOEJI
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    • v.27 no.4
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    • pp.289-293
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    • 1983
  • Twelve new N-piperoyl amino acids were synthesized by acylation of amino acids with piperoylchloride in order to develop the new central nervous depressants. Silylation of the carboxylic group of amino acids not only precluded side reactions but-also facilitated acylation at room temperature without catalysts. The acute toxicity of all the synthesized compounds were lower than that of piperine itself, whereas they showed strong protective effect against the strychnine-induced mortality.

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Syntheses and Antibacterial Activities of New Quinolones Containing cis- or trans-3-Amino-4-methylthiomethylpyrrolidino Moiety (시스 또는 트란스-3-아미노-4-메틸티오메틸피롤리디닐기를 포함하는 퀴놀론 항균물질의 합성과 효능검색)

  • Lee, Jae-Wook;Lim, Gui-Taek
    • Journal of Life Science
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    • v.13 no.6
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    • pp.943-949
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    • 2003
  • New quinolone derivatives of 7-(cis- or trans-3-amino-4-mehtylthiomethylpyrrolidinyl) quinolone-3-carboxylic acids were synthesized by condensation of 7-halo substituted quinolone-3-carboxylic acids with cis- or trans-3-amino-4-mehtylthiomethylpyrrolidine. Some of these compounds showed broad spectra of antibacterial activities against Gram-positive and Gram-negative organisms except Pseudomonas aeruginosa, and exhibited much stronger activity against MRSA.

The uptake of basic amino acids into fibroblasts was enhanced by PCA.

  • Ogasahara, Kazuko;Takino, Yoshinobu;Sakamoto, Kazutami
    • Proceedings of the SCSK Conference
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    • 2003.09b
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    • pp.145-148
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    • 2003
  • Previously, we reported that L-PCA enhanced blood circulation by modulating constitutive NO production. It was that L-PCA increased L-Arg uptake into endothelial cell, followed by the enhancement of NO production. Then we recommended the use of L-PCA for cosmetics, not only as humectants but also as enhancer of blood circulation. Since L-Arg is transported into endothelial cells by CAT (cationic amino acid transporter), it is expected that L-PCA also increase the uptake of basic amino acid, L-Lys. In this study, the uptakes of some amino acids into cells were evaluated by using 3H-labelled amino acid. Then we found the tendency that the uptake of L-Lys into endothelial cells was also enhanced by L-PCA. And the evident effect was observed in the epidermal fibroblasts, which had also CAT. Furthermore, it was found that the transportation of the other type of amino acids were not enhanced by L-PCA. That is to say, a famous moisturizer, L-PCA, has some effects on basic amino acid transport into cells.

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Effects of Ingredients of Wet Etchant on Glass Slimming Process (유리기판 박막화를 위한 습식공정에서 식각액 성분의 영향)

  • Shin, Young Sik;Lee, Won Gyu
    • Korean Chemical Engineering Research
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    • v.58 no.3
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    • pp.474-479
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    • 2020
  • The etching solution for slimming of glass substrates was manufactured and HF was used as the main ingredient of wet etching solutions. Various types of strong acids such as HCl, HNO3, H2SO4, amino acids and carboxylic acids such as citric acid, and etched solutions, respectively, were used to measure the etching rates and changes in surface shape of the glass. Regardless of the type of strong acids, the etching rate of the glass increased linearly as the added amount increased, and the sludge removal effect of the glass surface was also shown. The etching solution containing HCl showed more efficient results than other strong acids in the etching rate and the effect of removing sludge. The addition of carboxylic acid did not significantly affect the variation of etching rate, but had the effect of removing sludge. However, if amino acids were added, changes in etching rate and sludge removal were not significant.