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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ramazzotti M,Parrini C,Stefani M,Manao G,Degl'Innocenti Ddoi
10.1016/j.febslet.2006.11.033subject
Has Abstractpub_date
2006-12-22 00:00:00pages
6763-8issue
30eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01360-3journal_volume
580pub_type
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