FEBS Letters | |
Characterization of a novel Drosophila melanogaster acylphosphatase | |
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
【 预 览 】
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RO201912020312652ZK.pdf | 158KB | download |