TY  - GEN
AU  - Ramón-Maiques,S
AU  - Marina,A
AU  - Uriarte,M
AU  - Fita,I
AU  - Rubio,V
TI  - The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases
SN  - 0022-2836
PY  - 2000///0710
KW  - Adenosine Diphosphate
KW  - metabolism
KW  - Amino Acid Sequence
KW  - Binding Sites
KW  - Carbamyl Phosphate
KW  - Catalysis
KW  - Crystallography, X-Ray
KW  - Dimerization
KW  - Enterococcus faecalis
KW  - enzymology
KW  - Enzyme Stability
KW  - Kinetics
KW  - Models, Molecular
KW  - Molecular Sequence Data
KW  - Phosphotransferases (Carboxyl Group Acceptor)
KW  - chemistry
KW  - Protein Binding
KW  - Protein Structure, Secondary
KW  - Protein Structure, Tertiary
KW  - Pyrococcus furiosus
KW  - Solvents
KW  - Static Electricity
KW  - Structure-Activity Relationship
KW  - Temperature
N1  - Publication Type: Journal Article; Research Support, Non-U.S. Gov't
UR  - https://doi.org/10.1006/jmbi.2000.3779
ER  -