The 1.5 Å 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 1 1Edited by R. Huber-Reference-Cited by-同舟云学术

The 1.5 Å 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 1 1Edited by R. Huber

Published:2000-06 Issue:2 Volume:299 Page:463-476
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Ramón-Maiques Santiago,Marina Alberto,Uriarte Matxalen,Fita Ignacio,Rubio Vicente

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference39 articles.

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5. The influence of effectors and subunit interactions on Escherichia coli carbamyl phosphate synthetase studied by differential scanning calorimetry;Cervera;J. Biol. Chem.,1993

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