Skip to main content
SpringerLink
Log in

Effect of Ketosubstrate on the Product Yield in the Transamination Reaction Catalyzed by Transaminase from Thermoproteus uzoniensis

  • BIOCHEMISTRY, BIOPHYSICS, AND MOLECULAR BIOLOGY
  • Published:
Doklady Biochemistry and Biophysics Aims and scope Submit manuscript

Abstract

The study of the equilibrium of reactions catalyzed by thermostable enzymes is in demand for the development of biotechnological enzyme processes. The results of the analysis of equilibrium of transamination reaction catalyzed by thermostable transaminase from the archaeon Thermoproteus uzoniensis are presented below. A comparison of the conversion of substrates was performed for reactions with L-leucine and pyruvate and L-leucine and 2-oxobutyrate at 65°C. The establishment of the equilibrium was controlled by a decrease in the concentration of 2-oxobutyrate or pyruvate and by the accumulation of the keto analog of L-leucine. It was shown that the degree of conversion of L-leucine in the reaction with specific 2-oxobutyrate is higher than in the reaction with nonspecific pyruvate.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1.
Fig. 2.

Similar content being viewed by others

REFERENCES

  1. Eliot, A.C. and Kirsch, J.F., Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations, Annu. Rev. Biochem., 2004, vol. 73, pp. 383–415. https://doi.org/10.1146/annurev.biochem.73.011303.-074021

    Article  CAS  PubMed  Google Scholar 

  2. Slabu, I., Galman, J.L., Lloyd, R.C., et al., Discovery, engineering, and synthetic application of transaminase biocatalysts, ACS Catal., 2017, vol. 7, pp. 8263–8284. https://doi.org/10.1021/acscatal.7b02686

    Article  CAS  Google Scholar 

  3. Savile, C.K., Janey, J.M., Mundorff, E.C., et al., Biocatalytic asymmetric synthesis of sitagliptin manufacture, Science, 2010, vol. 329, pp. 305–309. https://doi.org/10.1126/science.1188934

    Article  CAS  PubMed  Google Scholar 

  4. Peng, Z., Wong, J.W., Hansen, E.C., et al., Development of a concise, asymmetric synthesis of a smoothened receptor (SMO) inhibitor: enzymatic transamination of a 4-piperidinone with dynamic kinetic resolution, Org. Lett., 2014, vol. 16, pp. 860–863. https://doi.org/10.1021/ol403630g

    Article  CAS  PubMed  Google Scholar 

  5. Goldberg, R.N. and Tewari, Y.B., Thermodynamics of enzyme-catalyzed reactions: part 2. Transferases, J. Phys. Chem. Ref. Data, 1994, vol. 23, pp. 547–617. https://doi.org/10.1063/1.555948

    Article  CAS  Google Scholar 

  6. Tewari, Y.B., Kishore, N., Goldberg, R.N., et al., An equilibrium and calorimetric study of some transamination reactions, J. Chem. Thermodyn., 1998, vol. 30, pp. 777–793. https://doi.org/10.1006/jcht.1998.0342

    Article  CAS  Google Scholar 

  7. Cellini, B., Bertoldi, M., Montioli, R., et al., Human wild-type alanine: glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications, Biochem. J., 2007, vol. 408, pp. 39–50. https://doi.org/10.1042/BJ20070637

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Boyko, K.M., Stekhanova, T.N., Nikolaeva, A.Y., et al., First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines, Extremophiles, 2016, vol. 20, pp. 215–225.

    Article  CAS  Google Scholar 

  9. Bezsudnova, E.Y., Stekhanova, T.N., Suplatov, D.A., et al., Experimental and computational studies on the unusual substrate specificity of branched-chain amino acid aminotransferase from Thermoproteus uzoniensis,Arch. Biochem. Biophys., 2016, vol. 607, pp. 27–36. https://doi.org/10.1007/s00792-016-0816-z

    Article  CAS  PubMed  Google Scholar 

  10. Eisenthal, R., Danson, M.J., and Hough, D.W., Catalytic efficiency and kcat/Km: a useful comparator?, Trends Biotech., 2007, vol. 25, pp. 247–249. https://doi.org/10.1016/j.tibtech.2007.03.010

    Article  CAS  Google Scholar 

Download references

Funding

This work was partially supported by the Russian Science Foundation (project no. 19-14-00164, determination of the equilibrium constants and the degree of conversion).

Author information

Authors and Affiliations

  1. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia

    E. Yu. Bezsudnova, T. N. Stekhanova, K. M. Boyko &  V. O. Popov

  2. National Research Centre “Kurchatov Institute”, Moscow, Russia

    V. O. Popov

Authors
  1. E. Yu. Bezsudnova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. T. N. Stekhanova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. K. M. Boyko
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. V. O. Popov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to E. Yu. Bezsudnova.

Ethics declarations

The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.

Additional information

Translated by M. Batrukova

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Bezsudnova, E.Y., Stekhanova, T.N., Boyko, K.M. et al. Effect of Ketosubstrate on the Product Yield in the Transamination Reaction Catalyzed by Transaminase from Thermoproteus uzoniensis. Dokl Biochem Biophys 490, 5–8 (2020). https://doi.org/10.1134/S1607672920010020

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1607672920010020

Keywords:

Search

Navigation