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<article 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" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Acta Naturae</journal-id><journal-title-group><journal-title xml:lang="en">Acta Naturae</journal-title><trans-title-group xml:lang="ru"><trans-title>Acta Naturae</trans-title></trans-title-group></journal-title-group><issn publication-format="print">2075-8251</issn><publisher><publisher-name xml:lang="en">Acta Naturae Ltd</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">10755</article-id><article-id pub-id-type="doi">10.32607/20758251-2009-1-3-29-51</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>Articles</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>Статьи</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Chemical and Functional Aspects of Posttranslational Modification of Proteins</article-title><trans-title-group xml:lang="ru"><trans-title>Chemical and Functional Aspects of Posttranslational Modification of Proteins</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name><surname>Knorre</surname><given-names>D G</given-names></name><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Kudryashova</surname><given-names>N V</given-names></name><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Godovikova</surname><given-names>T S</given-names></name><email>godov@niboch.nsc.ru</email><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru"></institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2009-12-15" publication-format="electronic"><day>15</day><month>12</month><year>2009</year></pub-date><volume>1</volume><issue>3</issue><issue-title xml:lang="en">NO3 (2009)</issue-title><issue-title xml:lang="ru">№3 (2009)</issue-title><fpage>29</fpage><lpage>51</lpage><history><date date-type="received" iso-8601-date="2020-01-17"><day>17</day><month>01</month><year>2020</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2009, Knorre D.G., Kudryashova N.V., Godovikova T.S.</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2009, Knorre D.G., Kudryashova N.V., Godovikova T.S.</copyright-statement><copyright-year>2009</copyright-year><copyright-holder xml:lang="en">Knorre D.G., Kudryashova N.V., Godovikova T.S.</copyright-holder><copyright-holder xml:lang="ru">Knorre D.G., Kudryashova N.V., Godovikova T.S.</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/><license><ali:license_ref xmlns:ali="http://www.niso.org/schemas/ali/1.0/">https://creativecommons.org/licenses/by/4.0</ali:license_ref></license></permissions><self-uri xlink:href="https://actanaturae.ru/2075-8251/article/view/10755">https://actanaturae.ru/2075-8251/article/view/10755</self-uri><abstract xml:lang="en"><p/></abstract><trans-abstract xml:lang="ru"><p>This paper reviews the chemical and functional aspects of the posttranslational modifications of proteins, which are achieved by the addition of various groups to the side chain of the amino acid residue backbone of proteins. It describes the main prosthetic groups and the interaction of these groups and the apoenzyme in the process of catalysis, using pyridoxal catalysis as an example. Much attention is paid to the role of posttranslational modification of proteins in the regulation of biochemical processes in live organisms, and especially to the role of protein kinases and their respective phosphotases. Methylation and acetylation reactions and their role in the “histone code,” which regulates genome expression on the transcription level, are also reviewed. This paper also describes the modification of proteins by large hydrophobic residues and their role in the function of membrane-associated proteins. Much attention is paid to the glycosylation of proteins, which leads to the formation of glycoproteins. We also describe the main non-enzymatic protein modifications such as glycation, homocysteination, and desamidation of amide residues in dibasic acids.</p></trans-abstract><kwd-group xml:lang="en"><kwd>proteins</kwd><kwd>enzymes</kwd><kwd>posttranslational modification</kwd><kwd>prosthetic groups</kwd><kwd>posphorylation</kwd><kwd>regulation</kwd><kwd>signal transduction</kwd><kwd>acylation</kwd><kwd>alkylation</kwd><kwd>ubiquitinilation</kwd><kwd>histone code</kwd><kwd>non-fermentative modification</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Walsh C.T., Garneau-Tsodikova S., Gatto G.J. Angew. Chem. Int. Ed. 2005 V. 44. № 45. P. 7342–7372.</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Lehninger A. Principles of Biochemistry. New York: W.H. Freeman and Company. 2008.</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Karpeysky M.Y., Ivanov V.I. Nature. 1966. V. 210. № 30. 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