Characterization of a novel Drosophila melanogaster acylphosphatase

FEBS Letters

Chiti, Fabrizio¹  Raugei, Giovanni¹  Degl'Innocenti, Donatella¹  Ramponi, Giampietro¹  Ramazzotti, Matteo¹  Marzocchini, Riccardo¹ 

[1] Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy

关键词: Acylphosphatase;    Activity;    Protein stability;    Ancestor;    Drosophila;   

DOI  :  10.1016/S0014-5793(02)03901-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analysis of the Drosophila melanogaster EST database led to the characterization of a novel acylphosphatase (AcPDro2). This is coded by the CG18505 (Acyp2) gene and is clearly distinct from a previously described AcPDro coded by the CG16870 (Acyp) gene from D. melanogaster. The two proteins show a 60% homology with both vertebrate isoenzymes. All the residues involved in the catalytic mechanism are conserved. AcPDro2 is a stable enzyme with a correct globular folded structure. Its activity on benzoylphosphate shows higher K _cat but lower K _m with respect to AcPDro. It is possible that AcPDro and AcPDro2 genes are not the direct ancestor of MT and CT vertebrate isoenzymes.

【 授权许可】

Unknown