(Q28288969)

1

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J B Thoden

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G D Reinhart

3

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H M Holden

Current Opinion in Chemical Biology

4

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language of work or name

English

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publication date

October 1998

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published in

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volume

2

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page(s)

624-32

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issue

5

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cites work

Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product

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Quantifying the allosteric properties of Escherichia coli carbamyl phosphate synthetase: determination of thermodynamic linked-function parameters in an ordered kinetic mechanism

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Allosteric effects of carbamoyl phosphate synthetase from Escherichia coli are entropy-driven

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Phosphorus-31 nuclear magnetic resonance application to positional isotope exchange reactions catalyzed by Escherichia coli carbamoyl-phosphate synthetase: analysis of forward and reverse enzymatic reactions

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Determination of rate-limiting steps of Escherichia coli carbamoyl-phosphate synthase. Rapid quench and isotope partitioning experiments

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Novel mechanism for carbamoyl-phosphate synthetase: a nucleotide switch for functionally equivalent domains

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DNA sequence of the carA gene and the control region of carAB: tandem promoters, respectively controlled by arginine and the pyrimidines, regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia coli K-12.

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The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase

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A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity

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Kinetic mechanism of Escherichia coli carbamoyl-phosphate synthetase

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Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase

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Comparison of the functional differences for the homologous residues within the carboxy phosphate and carbamate domains of carbamoyl phosphate synthetase.

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Identification of critical amino acid residues of Saccharomyces cerevisiae carbamoyl-phosphate synthetase: definition of the ATP site involved in carboxy-phosphate formation.

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Differential roles for three conserved histidine residues within the large subunit of carbamoyl phosphate synthetase.

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Regulatory changes in the control of carbamoyl phosphate synthetase induced by truncation and mutagenesis of the allosteric binding domain

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Domain structure of the large subunit of Escherichia coli carbamoyl phosphate synthetase. Location of the binding site for the allosteric inhibitor UMP in the COOH-terminal domain.

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Detection of an enzyme bound gamma-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli

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Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase

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The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

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Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis

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Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase

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Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution

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Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution

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Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site

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Activation by fusion of the glutaminase and synthetase subunits of Escherichia coli carbamyl-phosphate synthetase.

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The smallest carbamoyl-phosphate synthetase. A single catalytic subdomain catalyzes all three partial reactions

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