Molecular evolution of enolase

• Autorzy: Piast M. , Kustrzeba-Wojcicka I. , Matusiewicz M. , Banas T.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

glycolysis; concerted evolution; enzyme; enolase; muscle-specific enolase; evolution; gene duplication; vertebrate; neuron-specific enolase; non-neuronal enolase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 2
• Opis fizyczny: p.507-513,fig.,ref.

Twórcy

autor

Piast M.

• Wroclaw Medical University, Wroclaw, Poland

autor

Kustrzeba-Wojcicka I.

autor

Matusiewicz M.

autor

Banas T.

Bibliografia

• Babbit PC, Hasson MS, Wedekind JE, Palmer DR, Barre WC, Reed GH, Rayment I, Ringe D, Kenyon GI, Gerlt JA (1996) The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry 35: 16489–16501.
• Banaś T, Gontero B, Drews VL Johnson SL, Marcus F, Kemp RG (1988) Reactivity of the thiol groups of Escherichia coli phosphofructo-1-kinase. Biochim Biophys Acta 957: 178–184.
• Baranowski T, Wolna E (1975) Enolase from human muscle. Methods Enzymol 42: 335–338.
• Baranowski T, Wolna E, Morawiecki A (1968) Purification and properties of crystalline 2-phospho—glycerate hydro-lyase from human muscle. Eur J Biochem 5: 119–123.
• Hannaert V, Brinkmann H, Nowitzki U, Lee JA, Albert MA, Sensen CW, Gaasterland T, Muller M, Michaels P, Martin W (2000) Enolase from Trypanosoma brucei from the amitochondriate protist Mastigamoeba balamuthi and from the chloroplast and cytosol of Euglena gracilis: pieces in the evolutionary puzzle of the eukaryotic glycolytic pathway. Mol Biol Evol 17: 989–1000.
• Kumar SK, Tamura I, Jakobsen B, Nei M (2001) MEGA2: Molecular evolutionary analysis so ware. Bioinformatics 17: 1244–1245.
• Kustrzeba-Wójcicka I, Golczak M (2000) Enolase from Candida albicans – purification and characterization. Comp Biochem Physiol 126 B: 109–120.
• Liao D (1999) Concerted evolution: molecular mechanism and biological implications. Am J Hum Genet 64: 24–30.
• Nei M, Kumar S (2000) Molecular Evolution and Phylogenetics, pp 10–13, Oxford University Press Oxford.
• Nei M, Gu X, Sitnikova T (1997) Evolution by the birthand- death process in multigene families of the vertebrate immune system. Proc Natl Acad Sci USA 94: 7799–7806.
• Ng P, Henikoff S (2001) Predicting deleterious amino acid substitutions. Genome Res 11: 863–874.
• Nitter-Marszalska M, Kustrzeba-Wójcicka I, Pisarczyk-Bogacka E, Medrala W, Patkowski J (1998) Skin test with enolase in the diagnosis of fungal allergy. Allergy 53: 30.
• Nowak K, Wolny M, Banaś T (1981) The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Le 134: 143–146.
• Pegg SC, Babbit PC (1999) Shotgun: geing more from sequence similarity searches. Bioinformatics 15: 729–740.
• Pietkiewicz J, Kustrzeba-Wójcicka I, Wolna E (1983) Purification and properties of enolase from carp (Cyprinus carpio). Comparison with enolases from mammals’ muscles and yeast. Comp Biochem Physiol 75B: 693–698.
• Piontkivska H, Rooney A, Nei M (2002) Puryfying selection and birth-and-death evolution in the histone H4 gene family. Mol Biol Evol 19: 689–697.
• Rider CC, Taylor CB (1975) Enolase isoenzymes. II. Hybridization studies developmental and phylogenetic aspects. Biochim Biophys Acta 405: 175–187.
• Rooney A Piontkivska H, Nei M (2002) Molecular evolution of the nontandemly repeated genes of the histone H3 multigene family. Mol Biol Evol 19: 68–75.
• Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406–425.
• Segil N, Shrutkowski A, Dworkin MB, Dowrkin-Rastl E (1988) Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence. Biochem J 251: 31–39.
• Stamm LV, Young NR (1997) Nucleotide sequence of the Treponema pallidum eno gene. DNA Seq 7: 261–265.
• Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876–4882.
• Tracy MR, Hedges SB (2000) Evolutionary history of the enolase gene family. Gene 259: 129–138.
• Van Der Straeten D, Rodrigues-Pousada RA, Goodman HM, Van Montagu M (1991) Plant enolase: gene structure expression and evolution. Plant Cell 3: 719–735.