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Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.
PLoS One. 2021 Jul 29;16(7):e0255098. doi: 10.1371/journal.pone.0255098. eCollection 2021.
PLoS One. 2021.
PMID: 34324538
Free PMC article.
The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme.
Bakunova AK, Nikolaeva AY, Rakitina TV, Isaikina TY, Khrenova MG, Boyko KM, Popov VO, Bezsudnova EY.
Bakunova AK, et al.
Molecules. 2021 Aug 20;26(16):5053. doi: 10.3390/molecules26165053.
Molecules. 2021.
PMID: 34443642
Free PMC article.
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Mechanistic aspects of the transamination reactions catalyzed by D-amino acid transaminase from Haliscomenobacter hydrossis.
Bakunova AK, Kostyukov AA, Kuzmin VA, Popov VO, Bezsudnova EY.
Bakunova AK, et al.
Biochim Biophys Acta Proteins Proteom. 2023 Feb 1;1871(2):140886. doi: 10.1016/j.bbapap.2022.140886. Epub 2022 Dec 7.
Biochim Biophys Acta Proteins Proteom. 2023.
PMID: 36496204
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Mechanism of D-Cycloserine Inhibition of D-Amino Acid Transaminase from Haliscomenobacter hydrossis.
Bakunova AK, Matyuta IO, Nikolaeva AY, Boyko KM, Popov VO, Bezsudnova EY.
Bakunova AK, et al.
Biochemistry (Mosc). 2023 May;88(5):687-697. doi: 10.1134/S0006297923050115.
Biochemistry (Mosc). 2023.
PMID: 37331714
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