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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
FEBS Lett.
|
| uniprot:author |
Chiti F.,
Degl'Innocenti D.,
Marzocchini R.,
Ramazzotti M.,
Ramponi G.,
Raugei G.
|
| uniprot:date |
2003
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| uniprot:pages |
171-174
|
| uniprot:title |
Characterization of a novel Drosophila melanogaster acylphosphatase.
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| uniprot:volume |
535
|
| dc-term:identifier |
doi:10.1016/S0014-5793(02)03901-7
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