СТРУКТУРНО-ФУНКЦИОНАЛЬНЫЙ АНАЛИЗ АМИНОКИСЛОТНЫХ ПОСЛЕДОВАТЕЛЬНОСТЕЙ ДАГФ-СИНТАЗЫ I ТИПА БАКТЕРИЙ PSEUDOMONAS SUBSP.CHLORORAPHIS AURANTIACA B-162
Аннотация
Цель исследования – структурно-функциональная характеристика аминокислотных последовательностей изоферментов ДАГФ-синтаз первого типа у штамма Pseudomonas chlororaphis subsp. aurantiaca B-162. Методы исследования: микробиологические, молекулярно-генетические, биоиформатические, методы филогенетического анализа.
Результаты. В ходе данного исследования в геноме бактерий P. chlororaphis subsp. aurantiaca В-162 было обнаружено две изоформы ДАГФ-синтаз Ia подтипа – DAHPIα1 и DAHPIα2. Сравнение нуклеотидных последовательностей этих ферментов показало 60% идентичности между ними. Анализ аминокислотных последовательностей DAHPIα1 и DAHPIα2 у бактерий P. chlororaphis subsp. aurantiaca В-162 продемонстрировал, что только DAHPIα2, содержит в своей структуре аллостерический сайт связывания тирозина. Второй фермент DAHPIα1 имеет неописанный в литературе консенсус, задействованный в формировании аллостерического сайта связывания неустановленного в настоящий момент регулятора.
Genome of P. chlororaphis subsp. aurantiaca B-162 encodes two isoforms of DAHP synthase Ia subtype, DAHPIα1 and DAHPIα2. Nucleotide sequences of these enzymes show 60% identity. Analysis of amino acid sequences of DAHPIα1 and DAHPIα2 from P chlororaphis subsp. aurantiaca B-162 demonstrated that only DAHPIα2 contains in its structure the allosteric site for tyrosine binding. DAHPIα1 enzyme has a consensus that is not described in the literature and that is involved in the formation of the allosteric binding site for unidentified regulator
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