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Crystal structure of NH
3
-dependent NAD
+
synthetase from Bacillus subtilis
Menico Rizzi
, Claudio Nessi
, Andrea Mattevi
, Alessandro Coda
, Martino Bolognesi
, Alessandro Galizzi
Research output
:
Contribution to journal
›
Article
›
peer-review
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3
-dependent NAD
+
synthetase from Bacillus subtilis'. Together they form a unique fingerprint.
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Keyphrases
Nicotinamide Adenine Dinucleotide (NAD+)
100%
Synthetase
100%
Bacillus Subtilis (B. subtilis)
100%
Pyrophosphate
33%
Catalytic Site
33%
ATP Synthase
16%
Glutamine
16%
3D Structure
16%
Mg2+
16%
X-ray Crystallography
16%
Homodimer
16%
Subunit Interface
16%
Tight
16%
Catalytic Center
16%
Catalyzed Reaction
16%
Freeform
16%
Structural Fingerprint
16%
NAD+ Binding
16%
Modification Methods
16%
Density Modification
16%
Switching Point
16%
GMP Synthetase
16%
Adenylation
16%
P-loop
16%
Multiple Isomorphous Replacement
16%
Biochemistry, Genetics and Molecular Biology
Adenosine Triphosphate
100%
Crystal Structure
100%
Pyrophosphate
66%
Enzyme
33%
Glutamine
33%
Anabolism
33%
Binding Site
33%
Nicotinamide Adenine Dinucleotide
33%
X-Ray Crystallography
33%
Guanosine Monophosphate
33%
Adenylylation
33%
Adenosine Monophosphate
33%