• 제목/요약/키워드: Amino-carboxyl acid

검색결과 84건 처리시간 0.023초

5-Hydroxy-2-phenylalanylaminomethyl-4-pyron 에 의한 티로시나제의 경쟁적 저해 (Competitive Inhibition of Tyrosinase by 5-Hydroxy-2-phenylalanylaminomethyl-4-pyron)

  • 임세진
    • 약학회지
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    • 제44권3호
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    • pp.279-282
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    • 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.

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$\etha$-N-[(2-Chloroethyl) nitrosocarbamoyl]-L-lysine의 합성 (Preparation of $\etha$-N-[(2-Chloroethyl) nitrosocarbamoyl]-L-lysine)

  • 김정균;조인섭
    • 약학회지
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    • 제27권2호
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    • pp.177-179
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    • 1983
  • A copper complex of $\epsilon$-N-[(2-chloroethyl)carbamoyl]-L-lysine was prepared by the treatment of the L-lysine copper complex with 2-chloroethyl isocyanate in cold water. Within the L-lysine copper complex molecule, the $\alpha-amino$ and carboxyl groups are bounded to $Cu^{2+}$ but the $\epsilon-amino$ group is free and can react with carbamoylating agents. A potential antitumor agent, $\epsilon-N-[(2-chloroethyl)$ nitrosocarbamoyl]-L-lysine was synthesized by nitrosation of this copper complex with Na $NO_{2}$ in anhydrous formic acid, followed by the passage of $H_{2}$S gas.

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Structural and Functional Importance of Two Glutamate Residues, Glu47 and Glu146, Conserved in N-Carbamyl D-Amino Acid Amodohydrolases

  • Oh, Ki-Hoon;Kim, Geun-Joong;Park, Joo-Ho;Kim, Hak-Sung
    • Journal of Microbiology and Biotechnology
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    • 제11권1호
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    • pp.29-34
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    • 2001
  • The mutant enzymes of N-carbamyl-D-amino aicd amidohydrolase (N-carbamylase) from Agrobacterium radiobacter NRRL B11291, showing a negligible activity, were selected from the library generated by random mutagenesis. From the sequence analysis, these mutants were found to contain the amino acids substitutions at Cys172, Glu47, and Glu146. Previously, Cys172 was reported to be necessary for the enzyme catalysis. The chemical modification of the N-carbamylase by carboxyl group specific chemical reagent, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide(EDC), resulted in a loss of activity. The replacement of glutamic acids with glutamines by site-directed mutagenesis led to aggregation of the enzymes. Mutant enzymes fused with maltose binding protein (MBP) were expressed in soluble form, but were inactive. These results indicate that two glutamic acid residues play an important role in structure and function of the N-carbamylase. Multiple sequence alignment of the related enzymes revealed that Glu47 and Glu146 are rigidly conserved, which suggests that tese residues are crucial for the structure and function of the functionally related C-N hydrolases.

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Effect of Antimicrobial Activity by Chitosan Oligosaccharide N-Conjugated with Asparagine

  • Jeon, You-Jin;Kim, Se-Kwon
    • Journal of Microbiology and Biotechnology
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    • 제11권2호
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    • pp.281-286
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    • 2001
  • Since the number of amino groups which are exposed by deacetylation of acetyl-D-glucosamine influences antimicrobial activity, a chitosan oligosaccharide (COS) derivative by N-conjugation of COS with asparagine, an amino acid with two amino groups, was synthesized and the antimicrobial effect on E. coli growth was compared with other COS derivatives which were N-conjugated with glycine, alanine, aspartic acid, cysteins, an methionine, and unmodified COS. The structure of asparagine N-conjugated COS (Asn-COS) derivative was identified by using a FT-IR, $^{13}C\;FT-NMR$, and an elemental analyzer. The antimicrobial activity of Asn-COS against E. coli growth was significantly improved as compared to the other COS derivatives as well as COS itself. This means that Asn-COS with two positive charges strongly interacts with the carboxyl negative charges on the bacteria cell wall. The results for Asn-COS were as follows: 100% bactericidal activity, 0.002% MIC, and no growth of E. coli during 3 days of culture time, suggesting that Asn-COS may be useful as a new antibiotic agent.

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Identification of Catalytic Amino Acid Residues by Chemical Modification in Dextranase

  • Ko, Jin-A;Nam, Seung-Hee;Kim, Doman;Lee, Jun-Ho;Kim, Young-Min
    • Journal of Microbiology and Biotechnology
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    • 제26권5호
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    • pp.837-845
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    • 2016
  • A novel endodextranase isolated from Paenibacillus sp. was found to produce isomaltotetraose and small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7-14 from dextran. To determine the active site, the enzyme was modified with 1-ethyl-3-[3-(dimethylamino)-propyl]-carbodiimide (EDC) and α-epoxyalkyl α-glucosides (EAGs), an affinity labeling reagent. The inactivation followed pseudo first-order kinetics. Kinetic analysis and chemical modification using EDC and EAGs indicated that carboxyl groups are essential for the enzymatic activity. Three Asp and one Glu residues were identified as candidate catalytic amino acids, since these residues are completely conserved across the GH family of 66 enzymes. Replacement of Asp189, Asp340, or Glu412 completely abolished the enzyme activity, indicating that these residues are essential for catalytic activity.

Molecular Design for the Formation of Two-dimensional Molecular Networks: STM Study of ${\gamma}$-phenylalanine on Au(111)

  • Jeon, A-Ram;Youn, Young-Sang;Lee, Hee-Seung;Kim, Se-Hun
    • 한국진공학회:학술대회논문집
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    • 한국진공학회 2011년도 제41회 하계 정기 학술대회 초록집
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    • pp.205-205
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    • 2011
  • The self-assembly of ${\gamma}$-phenylalanine on Au(111) at 150 K was investigated using scanning tunneling microscopy (STM). Phenylalanine can potentially form two-dimensional (2D) molecular networks through hydrogen bonding (through the carboxyl and amino groups) and ${\pi}-{\pi}$ stacking interactions (via aromatic rings). We found that ${\gamma}$-phenylalanine molecules self-assembled on Au(111) surfaces into well-ordered structures such as ring-shaped clusters (at low and intermediate coverages) and 2D molecular domains (intermediate and monolayer coverages), whereas ${\alpha}$-phenylalanine molecules formed less-ordered structure on Au(111). The self-assembly of ${\gamma}$- but not ${\alpha}$-phenylalanine may be related to the flexibility of the carboxyl and amino groups in the molecule. Moreover, as expected, the 2D molecular network of ${\gamma}$-phenylalanine on Au(111) was mediated by a combination of hydrogen bonding and ${\pi}-{\pi}$ stacking interactions.

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2염기산 무수물에 의한 양모섬유의 아실화(II) -아실화된 양모섬유의 성질을 중심으로- (Acylation of Wool Keratin with Dibasic Acid Anhydrides(II) ―on properties of acylated wool―)

  • Shin, Eun Joo;Park, Chan Hun;Choi, Suk Chul
    • 한국염색가공학회지
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    • 제8권2호
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    • pp.64-70
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    • 1996
  • Wool yarns were treated in dimethylformamide solutions containing various concntrations of three dibasic acid anhydrides: succinic, itaconic, and phthalic arthydrides in various conditions. The structurl aspects of these dibasic acid anhydries are different: succinic, itaconic, and phthalic acid arthydrides have saturated aliphatic ethylene, unsaturated aliphatic vinyl and aromatic phenyl one groups, respectively. The properties of acylated wool keratin are as follows: Decreasing amino group and increasing carboxyl group by acylation lowered the hydrophilic property, and then moisture regain, and decreased acid dye uptake and enhanced cationic dye uptake of wool keratin. In the case of phthalic acid anhydries, in spite of lowest acyl content, the minimum of moisture regain was resulted from the bulk benzen ring, occuping much more voids on wool keratin molecules than other reagents. Acid solubility was increased by the decrease of amino group and hydrogen bonding by acylation. Alkali solubility was also increased formation of new amide group on the side chain of keratin, which can be degraded easily by alkali. In the case of phthalic acid anhydride, the relative high solubility was resulted from the much higher molecular weight of dissolved fractions. The surface of wool keratin was not damaged by treatment with any acylating agent.

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Aspergillus nidulans에서 분리된 키틴 탈아세틸화 효소활성에 영향을 미치는 아미노산 잔기 분석 (Analysis of Amino Acid Residues Involved in Activities of Chitin Deacetylase of Aspergillus nidulans)

  • 김종일;송다현
    • 미생물학회지
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    • 제47권4호
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    • pp.302-307
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    • 2011
  • A. nidulans chitin deacetylase를 자가분해 용액으로부터 소수성 상호작용 컬럼 크로마토그래피와 이온 교환 컬럼 크로마토그래피를 통해 순수 분리하였다. 효소 활성에 관여하는 아미노산을 분석하기 위해 효소 단백질과 특정 아미노산 잔기에 작용하는 화학 수식제를 반응시켜 효소를 화학 수식하였다. histidine 잔기가 화학 수식된 효소는 효소활성을 100% 상실하였으며, arginine의 잔기 혹은 tyrosine 잔기는 100 ${\mu}M$보다 높은 농도의 수식제로 화학수식 되었을 때 효소활성이 감소하였다. Aspartic acid 혹은 glutamic acid의 carboxyl group 잔기의 화학수식은 효소활성의 상대적으로 작은감소를 나타냈다. 이것은 산성 아미노산의 잔기가 화학 촉매 반응에 직접 관여하지 않았거나 혹은 산성 아미노산 잔기는 효소단백질의 전반적인 구조에 영향을 미친다는 것을 추론할 수 있다. 이러한 결과는 효소 단백질의 촉매활성에 histidine, tyrosine 및 arginine 잔기가 중요한 역할을 담당하는 것을 의미한다.

배추과 식물현탁배양 세포내에서 산성 아미노산의 능동수송 (Active Transport of Acidic Amino Acids in Suspension Cultured Brassica sp. Cells)

  • 조봉희
    • 식물조직배양학회지
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    • 제22권3호
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    • pp.137-142
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    • 1995
  • 생리적인 pH에서 음전하를 띄우고 있는 산성 아미노산인 aspartate와 glutamate는 다른 중성 아미노산과 경쟁방해 실험을 행한 연구결과에 의하면 이들도 중성 아미노산이 갖는 능동운반계와 동일한 운반자를 소유한다. 중성 아미노산을 아미노산 한 분자 당 한개의 수소이온과 동반수송되고 전하에 보상을 위해서 한 분자 당 한개의 칼륨 이온을 배출한다. 그러나 산성 아미노산은 한 분자 당 2개의 수소이온과 동반수송되고, 한 분자 당 칼륨 한 분자를 배출한다. 중성 아미노산과 같은 운반계를 소유하고, 2개의 수소이온과 동반수송되는 능동운반계는 본 실험에서 처음으로 보고된다. 이 결과로부터 두개의 동반수송된 수소이온 중 한 개는 산성 아미노산에 있는 pK$_3$카르복실기를 먼저 중화시킨 후에 중성화된 형태로 수소이온 한 분자와 동반수송된다고 사료된다. 그러므로 유채는 20개의 아미노산에 대해서 다만 2개의 운반계, 즉 일반- 과 알카리성 아미노산 운반계를 가진 것으로 확인되었다. 다른 식물에서 이미 보고된 결과들을 참고하여 아미노산 운반계의 진화적인 의미를 고찰하였다.

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미생물의 색소에 관한 연구 제3보 -Tyrosine의 영향 - (Studies on the Microbial Pigment(III) -Tho Effect of Tyrosine-)

  • 안태석;민병예;홍순우
    • 미생물학회지
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    • 제16권1호
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    • pp.16-20
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    • 1978
  • 미생물의 색소형성에 관계한다고 보고된 8종의 amino acid 중에서 tyrosine 처리구에서만 색소가 형성되었다. 방사선 동위원소로 표시된 tyrosine과 2종의 돌연변이체를 사용하여 색소로의 전환 비율을 알아 본 결과, tyrosinem이 carboxyl기가 82%는 초기에 세포 대사물질로 쓰이며, 19%는 색소로 직접 전환이 되는 것을 알았다. 초기에 대사물질로 들어간 82%중 11%는 다시 색소로 전환된 것으로 측정되었다.

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