An Intermediate Complex in the Dissociation of Aspartate Transcarbamylase

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1974 Apr 1

PMID 4598300

Citations 7

Authors

D R Evans

W N Lipscomb

Affiliations

Soon will be listed here.

Abstract

The multisubunit enzyme aspartate transcarbamylase consists of six copies of two types of polypeptide chains, catalytic (C) and regulatory (R). A complex formed by the partial dissociation of this enzyme has been isolated. This species, which has the structure C(6)R(4), is a likely intermediate in the stepwise dissociation of aspartate transcarbamylase induced by mercurials. The formation of the complex is the result of the release of a single regulatory dimer (R(2)) from the parent molecule.The specific activity of the intermediate is essentially the same as that of aspartate transcarbamylase. By contrast, both homotropic and heterotropic interactions are reduced, but not abolished. These observations suggest that the allosteric transitions involved in the control mechanisms do not require the intact structure C(6)R(6).

Citing Articles

Protein complexes are under evolutionary selection to assemble via ordered pathways.

Marsh J, Hernandez H, Hall Z, Ahnert S, Perica T, Robinson C Cell. 2013; 153(2):461-70.

PMID: 23582331 PMC: 4009401. DOI: 10.1016/j.cell.2013.02.044.

A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits .

Mendes K, Kantrowitz E Biochemistry. 2010; 49(35):7694-703.

PMID: 20681545 PMC: 2935174. DOI: 10.1021/bi1010333.

Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase.

MOODY M, Vachette P, Foote A, Tardieu A, Koch M, BORDAS J Proc Natl Acad Sci U S A. 1980; 77(7):4040-3.

PMID: 6933451 PMC: 349764. DOI: 10.1073/pnas.77.7.4040.

Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: electron density at 5.9-angstroms resolution.

EDWARDS B, Evans D, Warren S, Monaco H, Landfear S, Eisele G Proc Natl Acad Sci U S A. 1974; 71(11):4437-41.

PMID: 4612518 PMC: 433901. DOI: 10.1073/pnas.71.11.4437.

Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.

Bothwell M, SCHACHMAN H Proc Natl Acad Sci U S A. 1974; 71(8):3221-5.

PMID: 4606892 PMC: 388655. DOI: 10.1073/pnas.71.8.3221.

References

Wiley D, Lipscomb W . Crystallographic determination of symmetry of aspartate transcarbamylase. Nature. 1968; 218(5147):1119-21. DOI: 10.1038/2181119a0. View

COOK R . Subunit interactions in aspartate transcarbamylase. Biochemistry. 1972; 11(20):3792-7. DOI: 10.1021/bi00770a019. View

Himes R, RABINOWITZ J . Formyltetrahydrofolate synthetase. II. Characteristics of the enzyme and the enzymic reaction. J Biol Chem. 1962; 237:2903-14. View

Rosenbusch J, Weber K . Subunit structure of aspartate transcarbamylase from Escherichia coli. J Biol Chem. 1971; 246(6):1644-57. View

GERHART J, SCHACHMAN H . Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry. 1968; 7(2):538-52. DOI: 10.1021/bi00842a600. View

Wiley D, Evans D, Warren S, McMurray C, EDWARDS B, Franks W . The 5.5 Angstrom resolution structure of the regulatory enzyme, asparate transcarbamylase. Cold Spring Harb Symp Quant Biol. 1972; 36:285-90. DOI: 10.1101/sqb.1972.036.01.038. View

Weber K . Aspartate transcarbamylase from Escherichia coli. Characterization of the polypeptide chains by molecular weight, amino acid composition, and amino-terminal residues. J Biol Chem. 1968; 243(3):543-6. View

Weber K . New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. Nature. 1968; 218(5147):1116-9. DOI: 10.1038/2181116a0. View

GERHART J, Pardee A . The enzymology of control by feedback inhibition. J Biol Chem. 1962; 237:891-6. View

10.

Warren S, EDWARDS B, Evans D, Wiley D, Lipscomb W . Aspartate transcarbamoylase from Escherichia coli: electron density at 5.5 A resolution. Proc Natl Acad Sci U S A. 1973; 70(4):1117-21. PMC: 433438. DOI: 10.1073/pnas.70.4.1117. View

11.

von Fellenberg R, Bethell M, Jones M, Levine L . Immunological studies of aspartate transcarbamylase. II. Effect of ligands on the conformation of the enzyme. Biochemistry. 1968; 7(12):4322-9. DOI: 10.1021/bi00852a026. View

12.

Markus G, McClintock D, Bussel J . Conformational changes in aspartate transcarbamylase. 3. A functional model for allosteric behavior. J Biol Chem. 1971; 246(3):762-71. View

13.

Richards K, Williams R . Electron microscopy of aspartate transcarbamylase and its catalytic subunit. Biochemistry. 1972; 11(18):3393-5. DOI: 10.1021/bi00768a012. View

14.

Changeux J, RUBIN M . Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux. Biochemistry. 1968; 7(2):553-61. DOI: 10.1021/bi00842a601. View

15.

Evans D, McMurray C, Lipscomb W . The thiol group in the catalytic chains of aspartate transcarbamoylase. Proc Natl Acad Sci U S A. 1972; 69(12):3638-42. PMC: 389838. DOI: 10.1073/pnas.69.12.3638. View

16.

Nelbach M, Pigiet Jr V, GERHART J, SCHACHMAN H . A role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli. Biochemistry. 1972; 11(3):315-27. DOI: 10.1021/bi00753a002. View

17.

GERHART J, Pardee A . ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION. Fed Proc. 1964; 23:727-35. View

18.

Jacobson G, Stark G . Aspartate transcarbamylase. A study of possible roles for the sulfhydryl group at the active site. J Biol Chem. 1973; 248(23):8003-14. View

19.

Matsumoto S, Hammes G . An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate. Biochemistry. 1973; 12(7):1388-94. DOI: 10.1021/bi00731a019. View

20.

Buckman T . Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation. Biochemistry. 1970; 9(16):3255-65. DOI: 10.1021/bi00818a020. View