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.

Autor:	Bakunova AK; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation., Matyuta IO; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation., Nikolaeva AY; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.; National Research Center 'Kurchatov Institute', Moscow, 123182 Russian Federation., Boyko KM; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation., Khomutov AR; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russian Federation., Bezsudnova EY; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation., Popov VO; Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.; Department of Biology, Lomonosov Moscow State University, Moscow, 119234 Russian Federation.
Jazyk:	angličtina
Zdroj:	Acta naturae [Acta Naturae] 2024 Jul-Sep; Vol. 16 (3), pp. 18-24.
DOI:	10.32607/actanaturae.27496
Abstrakt:	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. (Copyright ® 2024 National Research University Higher School of Economics.)
Databáze:	MEDLINE
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