Article (Scientific journals)
The CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase activity
Kupper, Michaël; Bauvois, Cédric; Frère, Jean-Marie et al.
2012In Extremophiles: Life Under Extreme Conditions, 16(1), p. 45-55
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Abstract :
[en] The CphAII protein from the hyperthermophile Aquifex aeolicus shows the five conserved motifs of the metallo-β-lactamase (MBL) superfamily and presents 28% identity with the Aeromonas hydrophila subclass B2 CphA MBL. The gene encoding CphAII was amplified by PCR from the A. aeolicus genomic DNA and overexpressed in Escherichia coli using a pLex-based expression system. The recombinant CphAII protein was purified by a combination of heating (to denature E. coli proteins) and two steps of immobilized metal affinity chromatography. The purified enzyme preparation did not exhibit a β-lactamase activity but showed a metal-dependent phosphodiesterase activity versus bis-p-nitrophenyl phosphate and thymidine 5'-monophosphate p-nitrophenyl ester, with an optimum at 85°C. The circular dichroism spectrum was in agreement with the percentage of secondary structures characteristic of the MBL αββα fold.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Kupper, Michaël;  Rheinisch - Westfälische Technische Hochschule Aachen - RWTH
Bauvois, Cédric;  Institut de recherches microbiologiques J.M. Wiame > Cristallographie des Protéines
Frère, Jean-Marie ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Galleni, Moreno ;  Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Bebrone, Carine ;  Rheinisch - Westfälische Technische Hochschule Aachen - RWTH
Language :
English
Title :
The CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase activity
Publication date :
January 2012
Journal title :
Extremophiles: Life Under Extreme Conditions
ISSN :
1431-0651
eISSN :
1433-4909
Publisher :
Springer Science & Business Media B.V., Tokyo, Japan
Volume :
16(1)
Pages :
45-55
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
BELSPO - SPP Politique scientifique - Service Public Fédéral de Programmation Politique scientifique
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
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