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Literature DB >> 22667327

A second allosteric site in Escherichia coli aspartate transcarbamoylase.

Alexis W Peterson¹, Gregory M Cockrell, Evan R Kantrowitz.

Abstract

Escherichia coli aspartate transcarbamoylase is feedback inhibited by CTP and UTP in the presence of CTP. Here, we show by X-ray crystallography that UTP binds to a unique site on each regulatory chain of the enzyme that is near but not overlapping with the known CTP site. These results bring into question all of the previously proposed mechanisms of allosteric regulation in aspartate transcarbamoylase.

Entities: Chemical Disease Mutation Species

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Year: 2012 PMID： 22667327 PMCID： PMC3428212 DOI： 10.1021/bi3006219

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

17 in total

1. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.

Authors: L Jin; B Stec; W N Lipscomb; E R Kantrowitz
Journal: Proteins Date: 1999-12-01

2. Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase.

Authors: P Suter; J P Rosenbusch
Journal: J Biol Chem Date: 1977-11-25 Impact factor: 5.157

3. Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model.

Authors: G J Howlett; M N Blackburn; J G Compton; H K Schachman
Journal: Biochemistry Date: 1977-11-15 Impact factor: 3.162

4. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.

Authors: J P Changeux; J C Gerhart; H K Schachman
Journal: Biochemistry Date: 1968-02 Impact factor: 3.162

5. Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.

Authors: J C Gerhart; H K Schachman
Journal: Biochemistry Date: 1965-06 Impact factor: 3.162

Review 6. Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.

Authors: Evan R Kantrowitz
Journal: Arch Biochem Biophys Date: 2011-12-16 Impact factor: 4.013

7. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution.

Authors: R C Stevens; J E Gouaux; W N Lipscomb
Journal: Biochemistry Date: 1990-08-21 Impact factor: 3.162

8. Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH.

Authors: J E Gouaux; R C Stevens; W N Lipscomb
Journal: Biochemistry Date: 1990-08-21 Impact factor: 3.162

9. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.

Authors: J R Wild; S J Loughrey-Chen; T S Corder
Journal: Proc Natl Acad Sci U S A Date: 1989-01 Impact factor: 11.205

10. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.

Authors: T S Corder; J R Wild
Journal: J Biol Chem Date: 1989-05-05 Impact factor: 5.157

5 in total

A second allosteric site in Escherichia coli aspartate transcarbamoylase.

1. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.

2. Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase.

3. Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model.

4. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.

5. Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.

Review 6. Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.

7. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution.

8. Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH.

9. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.

10. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.

Review 1. Solution NMR Spectroscopy for the Study of Enzyme Allostery.

2. Metal ion involvement in the allosteric mechanism of Escherichia coli aspartate transcarbamoylase.

3. ViewMotions Rainbow: a new method to illustrate molecular motions in proteins.

Review 4. From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.

5. Pyrimidine homeostasis is accomplished by directed overflow metabolism.