Characterization of a novel Drosophila melanogaster acylphosphatase

被引：15

作者：

Degl'Innocenti, D ^{[1
]}

Ramazzotti, M ^{[1
]}

Marzocchini, R ^{[1
]}

Chiti, F ^{[1
]}

Raugei, G ^{[1
]}

Ramponi, G ^{[1
]}

机构：

[1] Univ Florence, Dipartimento Sci Biochim, I-50134 Florence, Italy

来源：

FEBS LETTERS | 2003年 / 535卷 / 1-3期

关键词：

acylphosphatase; activity; protein stability; ancestor; Drosophila;

D O I：

10.1016/S0014-5793(02)03901-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 NIT and CT vertebrate isoenzymes. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：171 / 174

页数：4

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