8YRV
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid
Summary for 8YRV
| Entry DOI | 10.2210/pdb8yrv/pdb |
| Descriptor | Aminotransferase class IV, 3-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxypropanoic acid, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | daat, complex, transaminase, aminotransferase, d-amino acid, 3-aminooxypropionic acid, oxyme, transferase |
| Biological source | Haliscomenobacter hydrossis DSM 1100 |
| Total number of polymer chains | 1 |
| Total formula weight | 32680.32 |
| Authors | Matyuta, I.O.,Bakunova, A.K.,Nikolaeva, A.Y.,Popov, V.O.,Boyko, K.M. (deposition date: 2024-03-21, release date: 2024-04-17, Last modification date: 2024-12-18) |
| Primary citation | Bakunova, A.K.,Matyuta, I.O.,Nikolaeva, A.Y.,Boyko, K.M.,Khomutov, A.R.,Bezsudnova, E.Y.,Popov, V.O. Insights into the Functioning of the D-amino Acid Transaminase from Haliscomenobacter Hydrossis via a Structural and Spectral Analysis of its Complex with 3-Aminooxypropionic Acid. Acta Naturae, 16:18-24, 2024 Cited by PubMed Abstract: Pyridoxal 5'-phosphate-dependent enzymes play a crucial role in nitrogen metabolism. Carbonyl compounds, such as O-substituted hydroxylamines, stand out among numerous specific inhibitors of these enzymes, including those of practical importance, because they react with pyridoxal 5'-phosphate in the active site of the enzymes to form stable oximes. O-substituted hydroxylamines mimic the side group of amino acid substrates, thus providing highly potent and specific inhibition of the corresponding enzymes. The interaction between D-amino acid transaminase from bacterium and 3-aminooxypropionic acid was studied in the present work. The structural and spectral analyses of the complex of this transaminase with 3-aminooxypropionic acid allowed us to clarify some features of the organization and functioning of its active site and illustrate one of the mechanisms of inhibition by the specific substrate, D-glutamic acid. PubMed: 39539521DOI: 10.32607/actanaturae.27496 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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