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.

A K Bakunova, I O Matyuta, A Yu Nikolaeva, K M Boyko, A R Khomutov, E Yu Bezsudnova, V O Popov

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Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

7 authors.

A K BakunovaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

I O MatyutaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

A Yu NikolaevaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

K M BoykoBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

A R KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russian Federation.

E Yu BezsudnovaBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

V O PopovBach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, 119071 Russian Federation.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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

Indexed as

3-aminooxypropionic acidcrystal structureenzymatic catalysisinhibitortransaminase

Identifiers

PMID39539521

DOI10.32607/actanaturae.27496

PMCPMC11557217

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