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α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
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Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
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α-Alkylation of Ketones via Enolate Ions01:10

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Ketones with α protons are deprotonated by strong bases like lithium diisopropylamide (LDA) to form enolate ions. The anion is stabilized by resonance, and its hybrid structure exhibits negative charges on the carbonyl oxygen and the α carbon. This ambident nucleophile can attack an electrophile via two possible sites: the carbonyl oxygen, known as O-attack, or the α carbon, known as C-attack. The nucleophilic attack via the carbanionic site is preferred. This is due to the...
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Dipeptidyl Peptidase 4 Inhibitors01:23

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α-Alkylation of ketones is achieved in the presence of alkyl halides and a base. The reaction proceeds via the formation of an enolate ion followed by nucleophilic substitution. The choice of base employed is essential as it is the key factor in determining the reaction outcome.
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Nucleophilic substitution in α-halocarbonyl compounds can be achieved via an SN2 pathway. The reaction in α-haloketones is generally carried out with less basic nucleophiles. The use of strong basic nucleophiles leads to the generation of α-haloenolate ions, which often participate in other side reactions.
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L-Lysine-α-Oxidase: Acidovorax citrulli Bacterium Inhibitor.

I P Smirnova1, E V Karimova2, Yu A Shneider2

  • 1Medical Faculty, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia. smir-ip@yandex.ru.

Bulletin of Experimental Biology and Medicine
|March 6, 2018
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Summary

The fungus Trichoderma harzianum Rifai F-180

Keywords:
Acidovorax citrulliL-lysine-α-oxidase antitumor enzymeTrichoderma culture fluid

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Area of Science:

  • Microbiology
  • Enzymology
  • Biochemistry

Background:

  • The bacterium Acidovorax citrulli poses a significant threat to agriculture.
  • Enzymes produced by fungi show potential for antimicrobial applications.

Purpose of the Study:

  • To investigate the antibacterial activity of Trichoderma harzianum Rifai F-180 culture fluid concentrate and its L-lysine-α-oxidase enzyme against Acidovorax citrulli.

Main Methods:

  • Culturing Trichoderma harzianum Rifai F-180 in a specialized bioreactor.
  • Assaying the activity of L-lysine-α-oxidase in the culture fluid concentrate and the purified enzyme.

Main Results:

  • The culture fluid concentrate of Trichoderma harzianum Rifai F-180 exhibited antibacterial activity against Acidovorax citrulli.
  • The L-lysine-α-oxidase enzyme was successfully produced and quantified.

Conclusions:

  • Trichoderma harzianum Rifai F-180 produces an enzyme with potential antibacterial properties.
  • The findings suggest a possible biocontrol agent for Acidovorax citrulli infections.