PMID:17134700
| Citation |
Ramazzotti, M, Parrini, C, Stefani, M, Manao, G and Degl'Innocenti, D (2006) The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli. FEBS Lett. 580:6763-8 |
|---|---|
| Abstract |
Acylphosphatase (AcP) activity in prokaryotes was classically attributed to some aspecific acid phosphatases. We identified an open reading frame for a putative AcP in the b0968 Escherichia coli gene and purified the recombinant enzyme after checking by RT-PCR that it was indeed expressed. EcoAcP has a predicted typical fold of the AcP family but displays a very low specific activity and a high structural stability differently from its mesophilic and similarly to its hyperthermophilic counterparts. Site directed mutagenesis suggests that, together with other structural features, the intrachain S-S bridge in EcoAcP is involved in a remarkable thermal and chemical stabilization of the protein without affecting its catalytic activity. |
| Links |
PubMed Online version:10.1016/j.febslet.2006.11.033 |
| Keywords |
Acid Anhydride Hydrolases/genetics; Acid Anhydride Hydrolases/metabolism; Amino Acid Sequence; Animals; Circular Dichroism; Cysteine/genetics; Cysteine/metabolism; Disulfides/metabolism; Enzyme Stability; Escherichia coli/enzymology; Escherichia coli/genetics; Humans; Isoenzymes/metabolism; Molecular Sequence Data; Mutation/genetics; Protein Denaturation/drug effects; Sequence Alignment; Temperature; Thermodynamics; Urea/pharmacology |
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