Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa

Тип публикации: статья из журнала

Год издания: 2017

Идентификатор DOI: 10.1111/php.12694

Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity. © 2016 American Society for Photobiology.

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Издание

ISSN журнала: 00318655

Авторы

  • Larionova M.D. (Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation, Chair of Biophysics, Siberian Federal University, Krasnoyarsk, Russian Federation)
  • Markova S.V. (Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation, Chair of Biophysics, Siberian Federal University, Krasnoyarsk, Russian Federation)
  • Vysotski E.S. (Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation, Chair of Biophysics, Siberian Federal University, Krasnoyarsk, Russian Federation)

Вхождение в базы данных

  • Scopus (цитирований 4)
  • РИНЦ (eLIBRARY.RU) (цитирований 3)
  • Ядро РИНЦ (eLIBRARY.RU)
  • Web of Science Core Collection

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