S. A. Shilova, I. O. Matyuta, E. Y. Bezsudnova, M. E. Minyaev, A. Y. Nikolaeva, V. O. Popov, K. M. Boyko
{"title":"大肠杆菌中的 D-А 氨基酸Т转氨酶与 D-环丝氨酸复合物的 3D 结构","authors":"S. A. Shilova, I. O. Matyuta, E. Y. Bezsudnova, M. E. Minyaev, A. Y. Nikolaeva, V. O. Popov, K. M. Boyko","doi":"10.1134/s1063774523600916","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>D-cycloserine inhibits pyridoxal 5'-phosphate (PLP)-dependent enzymes both reversibly and irreversibly. As an alanine racemase inhibitor, D-cycloserine is used in drug therapy in the treatment of tuberculosis. Several products of the interaction of D-cycloserine and PLP in the active site of the enzyme are known. The crystal structure of the complex of PLP-dependent D-amino acid transaminase from the bacteria <i>Aminobacterium colombiense</i> (Amico) with D-cycloserine obtained at a resolution of 1.9 Å is presented, in which the ring-opened adduct of PLP and D-cycloserine was discovered. In addition, the interaction of D-cycloserine with Amico has been characterized by the kinetic and spectral methods, various products of the interaction of D-cycloserine and PLP in the active site of transaminase have been determined, and the coordination of D-cycloserine and PLP adducts in the Amico active site has been analyzed. It is established that the products of the interaction of D-cycloserine with PLP in the Amico active site are several compounds, including PLP and DCS adducts in the cyclic and open forms, oxime formed by PMP and β-aminooxy-D-alanine, and PMP and β-aminooxypyruvate.</p>","PeriodicalId":527,"journal":{"name":"Crystallography Reports","volume":null,"pages":null},"PeriodicalIF":0.6000,"publicationDate":"2024-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"3D Structure of D-Аmino Acid Тransaminase from Aminobacterium colombiense in Complex with D-Cycloserine\",\"authors\":\"S. A. Shilova, I. O. Matyuta, E. Y. Bezsudnova, M. E. Minyaev, A. Y. Nikolaeva, V. O. Popov, K. M. Boyko\",\"doi\":\"10.1134/s1063774523600916\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<h3 data-test=\\\"abstract-sub-heading\\\">Abstract</h3><p>D-cycloserine inhibits pyridoxal 5'-phosphate (PLP)-dependent enzymes both reversibly and irreversibly. As an alanine racemase inhibitor, D-cycloserine is used in drug therapy in the treatment of tuberculosis. Several products of the interaction of D-cycloserine and PLP in the active site of the enzyme are known. The crystal structure of the complex of PLP-dependent D-amino acid transaminase from the bacteria <i>Aminobacterium colombiense</i> (Amico) with D-cycloserine obtained at a resolution of 1.9 Å is presented, in which the ring-opened adduct of PLP and D-cycloserine was discovered. In addition, the interaction of D-cycloserine with Amico has been characterized by the kinetic and spectral methods, various products of the interaction of D-cycloserine and PLP in the active site of transaminase have been determined, and the coordination of D-cycloserine and PLP adducts in the Amico active site has been analyzed. It is established that the products of the interaction of D-cycloserine with PLP in the Amico active site are several compounds, including PLP and DCS adducts in the cyclic and open forms, oxime formed by PMP and β-aminooxy-D-alanine, and PMP and β-aminooxypyruvate.</p>\",\"PeriodicalId\":527,\"journal\":{\"name\":\"Crystallography Reports\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.6000,\"publicationDate\":\"2024-02-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Crystallography Reports\",\"FirstCategoryId\":\"88\",\"ListUrlMain\":\"https://doi.org/10.1134/s1063774523600916\",\"RegionNum\":4,\"RegionCategory\":\"材料科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CRYSTALLOGRAPHY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Crystallography Reports","FirstCategoryId":"88","ListUrlMain":"https://doi.org/10.1134/s1063774523600916","RegionNum":4,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CRYSTALLOGRAPHY","Score":null,"Total":0}
3D Structure of D-Аmino Acid Тransaminase from Aminobacterium colombiense in Complex with D-Cycloserine
Abstract
D-cycloserine inhibits pyridoxal 5'-phosphate (PLP)-dependent enzymes both reversibly and irreversibly. As an alanine racemase inhibitor, D-cycloserine is used in drug therapy in the treatment of tuberculosis. Several products of the interaction of D-cycloserine and PLP in the active site of the enzyme are known. The crystal structure of the complex of PLP-dependent D-amino acid transaminase from the bacteria Aminobacterium colombiense (Amico) with D-cycloserine obtained at a resolution of 1.9 Å is presented, in which the ring-opened adduct of PLP and D-cycloserine was discovered. In addition, the interaction of D-cycloserine with Amico has been characterized by the kinetic and spectral methods, various products of the interaction of D-cycloserine and PLP in the active site of transaminase have been determined, and the coordination of D-cycloserine and PLP adducts in the Amico active site has been analyzed. It is established that the products of the interaction of D-cycloserine with PLP in the Amico active site are several compounds, including PLP and DCS adducts in the cyclic and open forms, oxime formed by PMP and β-aminooxy-D-alanine, and PMP and β-aminooxypyruvate.
期刊介绍:
Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.