Тип публикации: статья из журнала

Год издания: 2016

Идентификатор DOI: 10.1093/bioinformatics/btw386

Аннотация: Motivation: Bacterial luciferases are heterodimeric enzymes that catalyze a chemical reaction, so called bioluminescence, which causes light emission in bacteria. Bioluminescence is vastly used as a reporter system in research tools and commercial developments. However, the details of the mechanisms that stabilize and transform theПоказать полностьюreaction intermediates as well as differences in the enzymatic kinetics amongst different bacterial luciferases remain to be elucidated. Results: Amino acid sequences alignments for 21 bacterial luciferases (both alpha- and beta-subunits) were analyzed. For alpha-subunit, containing the enzyme active center, 48 polymorphic amino acid positions were identified. According to them, the sequences fell into two distinct groups known as slow and fast based on the decay rate of the bioluminescence reaction. The differences in the enzyme active site induced by structural polymorphism are analyzed.

Журнал: BIOINFORMATICS

Выпуск журнала: Vol. 32, Is. 20

Номера страниц: 3053-3057

ISSN журнала: 13674803

Место издания: OXFORD

Издатель: OXFORD UNIV PRESS

• Deeva Anna A. (Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia)
• Temlyakova Evgenia A. (Inst Cell Biophys RAS, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia)
• Sorokin Anatoly A. (Inst Cell Biophys RAS, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia; Moscow Inst Phys & Technol, Dolgoprudnyi, Russia)
• Nemtseva Elena V. (Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia; Inst Biophys SB RAS, Lab Photobiol, Krasnoyarsk, Russia)
• Kratasyuk Valentina A. (Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia; Inst Biophys SB RAS, Lab Photobiol, Krasnoyarsk, Russia)

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