Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346

Biochemistry ◽  
1991 ◽  
Vol 30 (10) ◽  
pp. 2619-2624 ◽  
Author(s):  
Elisabeth Labruyere ◽  
Michele Mock ◽  
Witold K. Surewicz ◽  
Henry H. Mantsch ◽  
Thierry Rose ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Ligand Binding ◽  
Bacillus Anthracis ◽  
Truncated Form ◽  
Binding Properties

Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclase

Biochemistry ◽  
1990 ◽  
Vol 29 (20) ◽  
pp. 4922-4928 ◽  
Author(s):  
Elisabeth Labruyere ◽  
Michele Mock ◽  
Daniel Ladant ◽  
Susan Michelson ◽  
Anne Marie Gilles ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Bacillus Anthracis ◽  
Truncated Form ◽  
Binding Properties ◽  
Calmodulin Binding

scholarly journals Analysis of the contribution of the globin and reductase domains to the ligand-binding properties of bacterial haemoglobins

2007 ◽  
Vol 407 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Judith Farrés ◽  
Susanna Burckhardt-Herold ◽  
Jan Scherrer ◽  
Alexander D. Frey ◽  
Pauli T. Kallio
Keyword(s):  
Nitric Oxide ◽  
Carbon Monoxide ◽  
Fusion Protein ◽  
Ligand Binding ◽  
Rate Constants ◽  
Ralstonia Eutropha ◽  
Solvent Accessibility ◽  
Truncated Form ◽  
Binding Properties ◽  
Reductase Domain

Bacterial Hbs (haemoglobins), like VHb (Vitreoscilla sp. Hb), and flavoHbs (flavohaemoglobins), such as FHP (Ralstonia eutropha flavoHb), have different autoxidation and ligand-binding rates. To determine the influence of each domain of flavoHbs on ligand binding, we have studied the kinetic ligand-binding properties of oxygen, carbon monoxide and nitric oxide to the chimaeric proteins, FHPg (truncated form of FHP comprising the globin domain alone) and VHb-Red (fusion protein between VHb and the C-terminal reductase domain of FHP) and compared them with those of their natural counterparts, FHP and VHb. Moreover, we also analysed polarity and solvent accessibility to the haem pocket of these proteins. The rate constants for the engineered proteins, VHb-Red and FHPg, do not differ significantly from those of their natural counterparts, VHb and FHP respectively. Our results suggest that the globin domain structure controls the reactivity towards oxygen, carbon monoxide and nitric oxide. The presence or absence of a reductase domain does not affect the affinity to these ligands.

scholarly journals Characterization of a synthetic calmodulin-binding peptide derived from Bacillus anthracis adenylate cyclase.

1993 ◽  
Vol 268 (3) ◽  
pp. 1695-1701
Author(s):  
H. Munier ◽  
F.J. Blanco ◽  
B. Prêcheur ◽  
E. Diesis ◽  
J.L. Nieto ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Bacillus Anthracis ◽  
Binding Peptide ◽  
Calmodulin Binding

Ligand binding properties of the haem group

Nature ◽  
1977 ◽  
Vol 265 (5589) ◽  
pp. 15-16 ◽  
Author(s):  
A. J. Thomson
Keyword(s):  
Ligand Binding ◽  
Binding Properties
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