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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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D-Amino Acid Transaminases: Structural Diversity, Catalytic Properties, and Potential Applications.

Alina K Bakunova1, Sofia A Shilova1, Vladimir O Popov1,2

  • 1Bach Institute of Biochemistry, Federal Research Centre "Fundamentals of Biotechnology", Russian Academy of Sciences, Moscow, 119071, Russia.

Biochemistry. Biokhimiia
|March 17, 2026
PubMed
Summary

Pyridoxal-5'-phosphate (PLP)-dependent D-amino acid transaminases (DATAs) are crucial biocatalysts for synthesizing D-amino acids. Their high stereoselectivity and open active sites enable applications in biocatalysis and the nitrogen cycle.

Keywords:
D-amino acid transaminase (DATA)D-stereoselective aminationbiocatalysisenzyme stabilitypyridoxal-5′-phosphate-dependent catalysisstructure–function relationshipsubstrate specificitythree-dimensional structuretransaminase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Biocatalysis

Background:

  • D-amino acid transaminases (DATAs) are pyridoxal-5 omino-phosphate (PLP)-dependent enzymes essential for D-amino acid synthesis.
  • These enzymes play a role in the nitrogen cycle in bacteria and plants.
  • DATAs exhibit a mechanism similar to aspartate aminotransferase, involving two half-reactions and a pyridoxamine-5 omino-phosphate intermediate.

Purpose of the Study:

  • To review the properties, structure, and relationships of DATAs.
  • To discuss the biotechnological applications of DATAs.
  • To highlight the unique characteristics of DATAs, including their broad substrate specificity and stereoselectivity.

Main Methods:

  • Literature review of existing studies on DATAs.
  • Analysis of enzyme structure and active site organization.
  • Characterization of DATAs with promiscuous activity.

Main Results:

  • DATAs are dimeric enzymes with an open active site crucial for substrate binding.
  • Despite broad substrate specificity, DATAs demonstrate high stereoselectivity, producing no detectable L-amino acid byproducts.
  • Promiscuous DATAs capable of acting on substrates lacking an α-carboxylate group, such as primary (R)-amines, have been identified.

Conclusions:

  • DATAs are promising biocatalysts for (R)-stereoselective amination in multienzyme cascades due to their stability and stereoselectivity.
  • The open active site configuration allows for the binding and conversion of bulky, non-natural substrates.
  • Understanding the structural differences between DATA groups can further optimize their biotechnological applications.