Molecular evolution of enolase

• Authors: Michał Piast , Irena Kustrzeba-Wójcicka , Małgorzata Matusiewicz , Teresa Banaś
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

concerted evolution; gene duplication; "birth and death" evolution; glycolysis; vertebrates evolution; enolase

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2005
• Volume: 52
• Issue: 2
• Pages: 507-513

Dates

published

2005

received

2004-10-13

revised

2005-01-24

accepted

2005-02-07

(unknown)

2005-05-15

Contributors

author

Michał Piast

• Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland

author

Irena Kustrzeba-Wójcicka

• Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland

author

Małgorzata Matusiewicz

• Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland

author

Teresa Banaś

• Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland

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