Drosophila melanogaster acylphosphatase: A common ancestor for acylphosphatase isoenzymes of vertebrate species

FEBS Letters

Raugei, Giovanni¹  Magherini, Francesca¹  Taddei, Niccolò¹  Ramponi, Giampietro¹  Bozzetti, Maria Pia²  Cecchi, Cristina¹  Pieri, Alessandro¹  Liguri, Gianfranco¹ 

[1] Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Florence, Italy;Istituto di Genetica, Università di Bari, Via Amendola 165/A, 70126 Bari, Italy

关键词: Acylphosphatase;    Human muscle acylphosphatase;    Drosophila;    MT-AcP;    muscle-type acylphosphatase;    CT-AcP;    common-type acylphosphatase;    AcPDro;    Drosophila melanogaster acylphosphatase;    Δ22;    Drosophila melanogaster acylphosphatase deletion mutant;    IPTG;    isopropylthiogalactoside;    ORF;    open reading frame;    RT-PCR;    reverse transcriptase polymerase chain reaction;    GST;    glutathione S-transferase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    UTR;    untranslated region;   

DOI  :  10.1016/S0014-5793(98)00912-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An open reading frame encoding a putative acylphosphatase was found in Drosophila melanogaster. The corresponding gene product shows 40% identity and 22 additional amino acid residues at the C-terminus as compared to muscle- and common-type human acylphosphatases. Moreover, all the residues involved in the catalytic mechanism of vertebrate enzymes are conserved in the D. melanogaster acylphosphatase. The D. melanogaster protein and a deletion mutant, similar in length to vertebrate acylphosphatases, were produced by cloning the corresponding cDNA in Escherichia coli. The wild-type enzyme is a protein with a well-established three-dimensional fold and a markedly reduced conformational stability as compared to vertebrate isoenzymes. The specific activity of the enzyme is significantly lower than that found in vertebrate enzymes though the substrate binding capability is basically unaltered. The deletion of 22 residues does not cause a significant change in k _cat, while affecting the apparent binding parameters. This work suggests that the genes encoding the vertebrate enzymes originate from an ancestor gene by duplication and subsequent evolution.

【 授权许可】

Unknown