Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that the Cu,Zn superoxide dismutase from Escherichia coli is monomeric irrespective of the buffer and of ionic strength. The catalytic activity of the recombinant enzyme is comparable with that of eukaryotic isoenzymes, indicating that the dimeric structure commonly found in Cu,Zn superoxide dismutases is not necessary to ensure efficient catalysis. The analysis of the amino acid sequences suggests that an altered interaction between subunits occurs in all bacterial Cu,Zn superoxide dismutases. The substitution of hydrophobia residues with charged ones at positions located at the dimer interface of all known Cu,Zn superoxide dismutases could be specifically responsible for the monomeric structure of the E. coli enzyme.

Battistoni, A., Folcarelli, S., Gabbianelli, R., Capo, C.r., Rotilio, G. (1996). The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration: Evidence for altered subunit interaction in all the bacteriocupreins. BIOCHEMICAL JOURNAL, 320(3), 713-716.

The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration: Evidence for altered subunit interaction in all the bacteriocupreins

BATTISTONI, ANDREA;CAPO, CONCETTA ROSA;ROTILIO, GIUSEPPE
1996-01-01

Abstract

Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that the Cu,Zn superoxide dismutase from Escherichia coli is monomeric irrespective of the buffer and of ionic strength. The catalytic activity of the recombinant enzyme is comparable with that of eukaryotic isoenzymes, indicating that the dimeric structure commonly found in Cu,Zn superoxide dismutases is not necessary to ensure efficient catalysis. The analysis of the amino acid sequences suggests that an altered interaction between subunits occurs in all bacterial Cu,Zn superoxide dismutases. The substitution of hydrophobia residues with charged ones at positions located at the dimer interface of all known Cu,Zn superoxide dismutases could be specifically responsible for the monomeric structure of the E. coli enzyme.
1996
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
bacterial enzyme; copper zinc superoxide dismutase; monomer; recombinant protein; amino acid sequence; amino acid substitution; article; enzyme activity; enzyme structure; enzyme subunit; escherichia coli; gel filtration chromatography; nonhuman; priority journal; protein quaternary structure; Amino Acid Sequence; Animals; Cattle; Chromatography, Gel; Cloning, Molecular; Dimerization; DNA Primers; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Expression; Molecular Sequence Data; Protein Conformation; Recombinant Proteins; Sequence Alignment; Sequence Analysis; Superoxide Dismutase; Bacteria (microorganisms); Escherichia coli; Eukaryota
Battistoni, A., Folcarelli, S., Gabbianelli, R., Capo, C.r., Rotilio, G. (1996). The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration: Evidence for altered subunit interaction in all the bacteriocupreins. BIOCHEMICAL JOURNAL, 320(3), 713-716.
Battistoni, A; Folcarelli, S; Gabbianelli, R; Capo, Cr; Rotilio, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/55113
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