8yrv | pdb_00008yrv

Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid

spinqualitylabelsall models 8yrv, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8yrv is a 1 chain structure with sequence from Haliscomenobacter hydrossis DSM 1100. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: MG, OCF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F4KWH0_HALH1 Publication Abstract from PubMed 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 Haliscomenobacter hydrossis 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. 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.,Bakunova AK, Matyuta IO, Nikolaeva AY, Boyko KM, Khomutov AR, Bezsudnova EY, Popov VO Acta Naturae. 2024 Jul-Sep;16(3):18-24. doi: 10.32607/actanaturae.27496. PMID:39539521 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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