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<article article-type="review-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">biologyscience</journal-id><journal-title-group><journal-title xml:lang="ru">Тимирязевский биологический журнал</journal-title><trans-title-group xml:lang="en"><trans-title>Timiryazev Biological Journal</trans-title></trans-title-group></journal-title-group><issn pub-type="epub">2949-4710</issn><publisher><publisher-name>ФГБОУ ВО РГАУ-МСХА имени К.А. Тимирязева (ФГБОУ ВО РГАУ-МСХА имени К.А. Тимирязева)</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.26897/2949-4710-2024-2-3-61-68</article-id><article-id custom-type="elpub" pub-id-type="custom">biologyscience-172</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>3 - ГЕНЕТИКА, БИОТЕХНОЛОГИЯ, БИОХИМИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>3 - GENETICS, BIOTECHNOLOGY, BIOCHEMISTRY</subject></subj-group></article-categories><title-group><article-title>Подвергается ли дезаминированию антраниловая кислота в животном организме?</article-title><trans-title-group xml:lang="en"><trans-title>Is anthranil acid subject to deamination in animals?</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Малиновский</surname><given-names>А. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Malinovsky</surname><given-names>A. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Андрей Владленович Малиновский, инженер-технолог</p><p>197183, г. Санкт-Петербург, ул. Сабировская, д. 37</p></bio><bio xml:lang="en"><p>Andrey V. Malinovsky, Technical Engineer</p><p>37 Sabirovskaya St., St. Petersburg, 197183</p></bio><email xlink:type="simple">malinovskiy.andrey@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Специальное конструкторское технологическое бюро (СКТБ) «Биофизприбор» – Санкт-Петербургский филиал Федерального государственного унитарного предприятия «Экспериментально-производственные мастерские» Федерального медико-биологического агентства</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Special Design Technological Bureau (SDTB) “Biofizpribor”, St. Petersburg branch of the Federal State Unitary Enterprise “Experimental and Production Workshops” of Federal Biomedical Agency</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2024</year></pub-date><pub-date pub-type="epub"><day>19</day><month>12</month><year>2024</year></pub-date><volume>2</volume><issue>3</issue><fpage>61</fpage><lpage>68</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Малиновский А.В., 2025</copyright-statement><copyright-year>2025</copyright-year><copyright-holder xml:lang="ru">Малиновский А.В.</copyright-holder><copyright-holder xml:lang="en">Malinovsky A.V.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.bioscience-journal.com/jour/article/view/172">https://www.bioscience-journal.com/jour/article/view/172</self-uri><abstract><p>Все пути превращения природных аминокислот приводят к циклу Кребса. Но в последний могут поступать только безазотистые ациклические соединения. Однако в животном организме продукты дезаминирования и дециклизации аминокислот не только окисляются в цикле Кребса до конечных продуктов, но и превращаются в глюкозу и кетоновые тела. Следовательно, любая природная аминокислота обладает глюкогенным либо кетогенным действием, а некоторые аминокислоты обладают глюкокетогенным, или смешанным действием, так как в процессе распада образуют и продукт с глюкогенным действием, и продукт с кетогенным действием. К таким аминокислотам относится триптофан. Одним из продуктов распада триптофана является антраниловая кислота, причем если превращение другого продукта распада триптофана-3-гидроксиантраниловой кислоты давно хорошо известно и является причиной кетогенного действия триптофана, то превращение антраниловой кислоты долго оставалось неясным. Это порождало различные суждения, не позволяющие делать истинные заключения о действии антраниловой кислоты (глюкогенное или кетогенное), а следовательно, окончательные выводы о действии триптофана в животном организме. В статье приведен анализ превращения антраниловой кислоты в животном организме, что позволяет сделать вывод о метаболическом пути триптофана через нее. Показана невозможность прямого дезаминирования антраниловой кислоты у животных с вытекающим из прямого дезаминирования наличием глюкогенного действия антраниловой кислоты, а также кетогенное действие антраниловой кислоты вследствие ее окисления в 3-гидроксиантраниловую кислоту. А поскольку обе кислоты являются промежуточными продуктами распада белковой аминокислоты триптофана, этот факт должен учитываться в рационе животных в норме и патологии.</p></abstract><trans-abstract xml:lang="en"><p>All metabolic pathways of natural amino acids lead to the Krebs cycle. However, only nitrogen-free acyclic compounds can enter the Krebs cycle. In animals, however, the products of deamination and decyclization of amino acids are not only oxidized to end products in the Krebs cycle, but are also converted to glucose and ketone bodies. Consequently, every natural amino acid has a glucogenic or ketogenic effect, and some amino acids have a glucoketogenic or mixed effect, because they form both a glucogenic and a ketogenic product in the process of degradation. Tryptophan is such an amino acid. One of the degradation products of tryptophan is anthranilic acid. While the conversion of another degradation product of tryptophan, 3-hydroxyanthranilic acid, has long been known and is the cause of the ketogenic effect of tryptophan, the conversion of anthranilic acid has long remained unclear. This has led to various judgments that have not allowed true conclusions about the action of anthranilic acid (glucogenic or ketogenic) and, consequently, the final judgments about the action of tryptophan in animals. The article analyzes the conversion of anthranilic acid in animals, which allows us to conclude about the metabolic pathway of tryptophan through it. The article shows the impossibility of direct deamination of anthranilic acid in animals with the glucogenic effect of anthranilic acid resulting from direct deamination, and also shows the ketogenic effect of anthranilic acid due to its oxidation to 3-hydroxyanthranilic acid. Since both acids are intermediates in the degradation of the protein amino acid tryptophan, this fact should be taken into account in the diets of normal and pathological animals.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>антраниловая кислота</kwd><kwd>триптофан</kwd><kwd>дезаминирование</kwd><kwd>кетоз</kwd><kwd>животные</kwd><kwd>дезаминирование антраниловой кислоты</kwd></kwd-group><kwd-group xml:lang="en"><kwd>anthranilic acid</kwd><kwd>tryptophan</kwd><kwd>deamination</kwd><kwd>ketosis</kwd><kwd>animals</kwd><kwd>deamination of anthranilic acid</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Leninger A.L. Biochemistrey. New York Worth Publishers. 1975. 1104.</mixed-citation><mixed-citation xml:lang="en">Leninger A.L. Biochemistrey. 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