Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8384086 | FEBS Letters | 2006 | 6 Pages |
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.
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Authors
Matteo Ramazzotti, Claudia Parrini, Massimo Stefani, Giampaolo Manao, Donatella Degl'Innocenti,