Mechanism of the reaction catalyzed by carbamyl phosphate synthetase. Binding of ATP to the two functionally different ATP sites.-Reference-Cited by-同舟云学术

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Mechanism of the reaction catalyzed by carbamyl phosphate synthetase. Binding of ATP to the two functionally different ATP sites.

Published:1978-02 Issue:3 Volume:253 Page:800-803
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Powers S.G.,Meister A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference21 articles.

1. Evidence for an Activated Form of Carbon Dioxide in the Reaction Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*

2. Identification of enzyme-bound activated CO2 as carbonic-phosphoric anhydride: isolation of the corresponding trimethyl derivative from the active site of glutamine-dependent carbamyl phosphate synthetase.

3. Bicarbonate-Dependent Cleavage of Adenosine Triphosphate and Other Reactions Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*

4. Selective Inactivation of the Glutamine Binding Site of Escherichia coli Carbamyl Phosphate Synthetase by 2-Amino-4-oxo-5-chloropentanoic Acid*

5. Effect of potassium cyanate on the catalytic activities of carbamyl phosphate synthetase

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1. The Amidotransferases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

2. Structure and Mechanism of F0F1-Type ATP Synthases and ATPases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

3. Mechanism and Regulation of the Glutamine-Dependent Carbamyl Phosphate Synthetase ofEscherichia Coli;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

4. Positional Isotope Exchange Studies of Enzyme Mechanisms;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

5. Carbamoylphosphate Synthetase from Pseudomonas aeruginosa;European Journal of Biochemistry;2005-03-03

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