STRUCTURAL AND FUNCTIONAL ANALYSIS OF AMINOACID SEQUENCES OF 3-DEOXY-D- ARABINOHEPULOZONAT-7-PHOSPHATE SYNTHASE TYPE I FROM PSEUDOMONAS SUBSP. CHLORORAPIS AURANTIACA B-162
Abstract
The aim of the study is the structural and functional characteristics of the amino acid sequences of isoenzymes of DAGP synthases of the first type in the Pseudomonas chlororaphis subsp. aurantiaca B-162. Research methods: microbiological, molecular genetic, bioinformatics, phylogenetic analysis methods.
Results. In the course of this study, in the bacterial genome P. chlororaphis subsp. aurantiaca B-162, two isoforms of subtype Ia DAGP synthases, DAHPIα1 and DAHPIα2, were found. Comparison of the nucleotide sequences of these enzymes showed 60% identity between them. Analysis of amino acid sequences DAHPIα1 and DAHPIα2 in P. chlororaphis subsp. aurantiaca B-162 demonstrated that only DAHPIα2 contains an allosteric tyrosine binding site in its structure. The second enzyme DAHPIα1 has an undescribed consensus in the literature and is involved in the formation of an allosteric binding site for a currently unidentified regulator.
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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