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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/F4KWH0_HALH1 F4KWH0_HALH1] | [https://www.uniprot.org/uniprot/F4KWH0_HALH1 F4KWH0_HALH1] | ||
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== 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<ref>PMID:39539521</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||
Latest revision as of 09:40, 18 December 2024
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acidCrystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid
Structural highlights
FunctionPublication Abstract from PubMedPyridoxal 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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