Degl'Innocenti Donatella, Ramazzotti Matteo, Marzocchini Riccardo, Chiti Fabrizio, Raugei Giovanni, Ramponi Giampietro
Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy.
FEBS Lett. 2003 Jan 30;535(1-3):171-4. doi: 10.1016/s0014-5793(02)03901-7.
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.
对黑腹果蝇EST数据库的分析促成了一种新型酰基磷酸酶(AcPDro2)的鉴定。它由CG18505(Acyp2)基因编码,与先前描述的由黑腹果蝇CG16870(Acyp)基因编码的AcPDro明显不同。这两种蛋白质与脊椎动物的两种同工酶均显示出60%的同源性。参与催化机制的所有残基都是保守的。AcPDro2是一种稳定的酶,具有正确的球状折叠结构。相对于AcPDro,它对苯甲酰磷酸的活性表现出更高的催化常数(Kcat)但更低的米氏常数(Km)。AcPDro和AcPDro2基因有可能不是脊椎动物中肌型(MT)和心型(CT)同工酶的直接祖先。