{"id":15892,"date":"2022-06-29T11:11:41","date_gmt":"2022-06-29T04:11:41","guid":{"rendered":"https:\/\/bgrssb.icgbio.ru\/2022\/?p=15892"},"modified":"2022-09-20T10:32:31","modified_gmt":"2022-09-20T03:32:31","slug":"structure-features-of-novel-d-amino-acid-transaminase-from-aminobacterium-colombiense","status":"publish","type":"post","link":"https:\/\/bgrssb.icgbio.ru\/2022\/2022\/06\/29\/structure-features-of-novel-d-amino-acid-transaminase-from-aminobacterium-colombiense\/","title":{"rendered":"Structure features of novel D-amino acid transaminase from Aminobacterium colombiense"},"content":{"rendered":"<p><em>by Shilova S., Nikolaeva A., Rakitina T., Matuta I., Boyko K. , Bezsudnova E. | Bach Institute<\/em><br \/>\n<em>of Biochemistry, Research Centre of Biotechnology of the Russian Academy of Sciences, Moscow, Russia |<\/em><br \/>\n<em>Complex of NBICS Technologies, National Research Center \u201cKurchatov Institute\u201d, Moscow, Russia<\/em><\/p>\n<p>D-amino acid transaminases (DAATs) are pyridoxal-5&#8242;-phosphate-(PLP)-dependent enzymes<br \/>\nthat catalyze reversible and stereoselective transfer of the amino group between D-amino<br \/>\nacids and \u03b1-keto acids. DAATs belong to fold type IV of the PLP-dependent enzymes in<br \/>\nwhich the PLP forms a covalent bond with the catalytic Lys residue as well as a number of<br \/>\nnoncovalent conservative interactions among TAs of fold type IV. In the active site of known<br \/>\nDAATs, two modes of the organization of residues responsible for the substrate binding are<br \/>\nobserved. The first type is observed in the DAAT from Bacillus suptilis (bsDAAT, PDB ID:<br \/>\n3DAA), in which \u03b1-carboxylic group is bound by a &#8220;carboxylate trap&#8221; formed by three<br \/>\nresidues &#8211; Y31 from the \u03b2X-strand and R98*, H100* from the O-loop. The second type is<br \/>\nobserved in TAs from Curtobacterium pusillum (CpuTA, PDB ID: 5K3W) and<br \/>\nHaliscomenobacter hydrossis (Halhy, PDB ID: 7P7X): here the \u03b1-carboxylic group of<br \/>\nsubstrate is bound by two residues, R51*, K117 in CpuTA and R28*, R90 in Halhy. The R51*<br \/>\nand R28* residues are directed to the active site from the adjacent subunit, and the K117<br \/>\nand R90 residues are located on the \u03b2Y-strand. DAAT from Aminobacterium colombiense<br \/>\n(Amico) in the active site possesses residues similar to the bsDAAT (K99* and H101* on the<br \/>\nO-loop) and both CpuTA and Halhy (R27* and R88). To understand the Amico\u2019s active site<br \/>\norganization, structure of holo-form and the R88L variant were determined by the RSA.<\/p>\n<a href=\"https:\/\/bgrssb.icgbio.ru\/2022\/wp-content\/uploads\/sites\/3\/2022\/06\/ShilovaSA.pdf\" class=\"pdfemb-viewer\" style=\"\" data-width=\"max\" data-height=\"max\"  data-toolbar=\"bottom\" data-toolbar-fixed=\"off\">ShilovaSA<br\/><\/a>\n","protected":false},"excerpt":{"rendered":"<p>by Shilova S., Nikolaeva A., Rakitina T., Matuta I., Boyko K. , Bezsudnova E. | Bach Institute of Biochemistry, Research Centre of Biotechnology of the Russian Academy of Sciences, Moscow, Russia | Complex of NBICS Technologies, National Research Center \u201cKurchatov Institute\u201d, Moscow, Russia D-amino acid transaminases (DAATs) are pyridoxal-5&#8242;-phosphate-(PLP)-dependent enzymes that catalyze reversible and stereoselective [&hellip;]<\/p>\n","protected":false},"author":3967,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":[],"categories":[7],"tags":[247,248,249],"_links":{"self":[{"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/posts\/15892"}],"collection":[{"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/users\/3967"}],"replies":[{"embeddable":true,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/comments?post=15892"}],"version-history":[{"count":1,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/posts\/15892\/revisions"}],"predecessor-version":[{"id":15894,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/posts\/15892\/revisions\/15894"}],"wp:attachment":[{"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/media?parent=15892"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/categories?post=15892"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/bgrssb.icgbio.ru\/2022\/wp-json\/wp\/v2\/tags?post=15892"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}