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2005 | 52 | 2 | 507-513
Article title

Molecular evolution of enolase

Content
Title variants
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.
Publisher

Year
Volume
52
Issue
2
Pages
507-513
Physical description
Dates
published
2005
received
2004-10-13
revised
2005-01-24
accepted
2005-02-07
(unknown)
2005-05-15
Contributors
author
  • Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland
  • Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland
  • Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland
author
  • Department of Medical Biochemistry, Wrocław Medical University, Wrocław, Poland
References
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p507kz
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