- Tytuł:
- Molecular evolution of enolase
- Autorzy:
-
Piast, Michał
Kustrzeba-Wójcicka, Irena
Matusiewicz, Małgorzata
Banaś, Teresa - Powiązania:
- https://bibliotekanauki.pl/articles/1041439.pdf
- Data publikacji:
- 2005
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
concerted evolution
gene duplication
"birth and death" evolution
glycolysis
vertebrates evolution
enolase - Opis:
- Enolase (EC 4.2.1.11) is an enzyme of the glycolytic pathway catalyzing the dehydratation reaction of 2-phosphoglycerate. In vertebrates the enzyme exists in three isoforms: α, β and γ. The amino-acid and nucleotide sequences deposited in the GenBank and SwissProt databases were subjected to analysis using the following bioinformatic programs: ClustalX, GeneDoc, MEGA2 and S.I.F.T. (sort intolerant from tolerant). Phylogenetic trees of enolases created with the use of the MEGA2 program show evolutionary relationships and functional diversity of the three isoforms of enolase in vertebrates. On the basis of calculations and the phylogenetic trees it can be concluded that vertebrate enolase has evolved according to the "birth and death" model of evolution. An analysis of amino acid sequences of enolases: non-neuronal (NNE), neuron specific (NSE) and muscle specific (MSE) using the S.I.F.T. program indicated non-uniform number of possible substitutions. Tolerated substitutions occur most frequently in α-enolase, while the lowest number of substitutions has accumulated in γ-enolase, which may suggest that it is the most recently evolved isoenzyme of enolase in vertebrates.
- Źródło:
-
Acta Biochimica Polonica; 2005, 52, 2; 507-513
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł