The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.

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 Lett

journal_title

FEBS letters

authors

Ramazzotti M,Parrini C,Stefani M,Manao G,Degl'Innocenti D

doi

10.1016/j.febslet.2006.11.033

subject

Has Abstract

pub_date

2006-12-22 00:00:00

pages

6763-8

issue

30

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01360-3

journal_volume

580

pub_type

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