scholarly journals Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers.

1993 ◽  
Vol 59 (1) ◽  
pp. 250-254 ◽  
Author(s):  
R W Ye ◽  
M R Fries ◽  
S G Bezborodnikov ◽  
B A Averill ◽  
J M Tiedje
Keyword(s):  
Structural Gene ◽  
Nitrite Reductase ◽  
Gene Encoding

scholarly journals The Blue Copper-Containing Nitrite Reductase fromAlcaligenes xylosoxidans: Cloning of the nirAGene and Characterization of the Recombinant Enzyme

1999 ◽  
Vol 181 (8) ◽  
pp. 2323-2329 ◽  
Author(s):  
Miguel Prudêncio ◽  
Robert R. Eady ◽  
Gary Sawers
Keyword(s):  
Amino Acid ◽  
Nitrite Reductase ◽  
Recombinant Enzyme ◽  
Leader Peptide ◽  
Resonance Spectroscopy ◽  
Gene Encoding ◽  
Blue Copper

ABSTRACT The nirA gene encoding the blue dissimilatory nitrite reductase from Alcaligenes xylosoxidans has been cloned and sequenced. To our knowledge, this is the first report of the characterization of a gene encoding a blue copper-containing nitrite reductase. The deduced amino acid sequence exhibits a high degree of similarity to other copper-containing nitrite reductases from various bacterial sources. The full-length protein included a 24-amino-acid leader peptide. The nirA gene was overexpressed inEscherichia coli and was shown to be exported to the periplasm. Purification was achieved in a single step, and analysis of the recombinant Nir enzyme revealed that cleavage of the signal peptide occurred at a position identical to that for the native enzyme isolated from A. xylosoxidans. The recombinant Nir isolated directly was blue and trimeric and, on the basis of electron paramagnetic resonance spectroscopy and metal analysis, possessed only type 1 copper centers. This type 2-depleted enzyme preparation also had a low nitrite reductase enzyme activity. Incubation of the periplasmic fraction with copper sulfate prior to purification resulted in the isolation of an enzyme with a full complement of type 1 and type 2 copper centers and a high specific activity. The kinetic properties of the recombinant enzyme were indistinguishable from those of the native nitrite reductase isolated from A. xylosoxidans. This rapid isolation procedure will greatly facilitate genetic and biochemical characterization of both wild-type and mutant derivatives of this protein.

Identification and Characterization of a cDNA and the Structural Gene Encoding the Mouse Epithelial Membrane Protein-1

Genomics ◽  
1996 ◽  
Vol 36 (3) ◽  
pp. 379-387 ◽  
Author(s):  
Christian S. Lobsiger ◽  
Josef P. Magyar ◽  
Verdon Taylor ◽  
Philip Wulf ◽  
Andrew A. Welcher ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Gene ◽  
Gene Encoding ◽  
Identification And Characterization

Characterization of mutations that lie in the promoter-regulatory region for glnA, the structural gene encoding glutamine synthetase

1984 ◽  
Vol 197 (1) ◽  
pp. 150-160 ◽  
Author(s):  
Linda McCarter ◽  
Krystyna Krajewska-Grynkiewicz ◽  
Dzung Trinh ◽  
Grace Wei ◽  
Sydney Kustu
Keyword(s):  
Glutamine Synthetase ◽  
Structural Gene ◽  
Regulatory Region ◽  
Gene Encoding

scholarly journals Cloning and Biochemical Characterization of a Class A β-Lactamase from Prevotella intermedia

2001 ◽  
Vol 45 (8) ◽  
pp. 2386-2389 ◽  
Author(s):  
I. Madinier ◽  
T. Fosse ◽  
J. Giudicelli ◽  
R. Labia
Keyword(s):  
Structural Gene ◽  
Protein Sequence ◽  
Biochemical Characterization ◽  
Prevotella Intermedia ◽  
Gene Encoding ◽  
Class A

ABSTRACT The gene encoding a β-lactamase of Prevotella intermedia was cloned and sequenced. This gene, calledcfxA2, shared 98% identity with cfxA, the structural gene of a β-lactamase previously described inBacteroides vulgatus. The deduced protein sequence had a K272E substitution. CfxA2 had the characteristics of class A, group 2e β-lactamases.

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