The aspartate transcarbamoylase–dihydroorotase complex in Deinococcus radiophilus has an active dihydroorotase

Archives of Microbiology ◽

10.1007/s00203-005-0075-3 ◽

2006 ◽

Vol 185 (1) ◽

pp. 78-81 ◽

Author(s):

Donald McPhail ◽

Margaret Shepherdson

Keyword(s):

Aspartate Transcarbamoylase ◽

Deinococcus Radiophilus

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Faculty Opinions recommendation of Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.12818969.14100069 ◽

2011 ◽

Author(s):

Jean-Pierre Changeux

Keyword(s):

Escherichia Coli ◽

Time Evolution ◽

Quaternary Structure ◽

Tight Binding ◽

Aspartate Transcarbamoylase

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Aspartate Transcarbamoylase

RCSB Protein Data Bank ◽

10.2210/rcsb_pdb/mom_2017_11 ◽

2017 ◽

Author(s):

D.S. Goodsell

Keyword(s):

Aspartate Transcarbamoylase

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

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)40949-5 ◽

1977 ◽

Vol 252 (22) ◽

pp. 8136-8141 ◽

Author(s):

P. Suter ◽

J.P. Rosenbusch

Keyword(s):

Aspartate Transcarbamoylase

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Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85977-x ◽

1980 ◽

Vol 255 (5) ◽

pp. 1962-1970 ◽

Author(s):

M.A. Bothwell ◽

H.K. Schachman

Keyword(s):

Kinetic Studies ◽

Aspartate Transcarbamoylase ◽

Regulatory Subunits

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Crystallization and preliminary X-ray diffraction studies of an inactive mutant aspartate transcarbamoylase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)69302-6 ◽

1981 ◽

Vol 256 (10) ◽

pp. 4691-4692

Author(s):

R. Kim ◽

T.S. Young ◽

H.K. Schachman ◽

S.H. Kim

Keyword(s):

Escherichia Coli ◽

Aspartate Transcarbamoylase ◽

X Ray Diffraction ◽

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Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)69358-0 ◽

1981 ◽

Vol 256 (10) ◽

pp. 5005-5015

Author(s):

A. Shrake ◽

A. Ginsburg ◽

H.K. Schachman

Keyword(s):

Escherichia Coli ◽

Conformational Transition ◽

Enthalpy Change ◽

Aspartate Transcarbamoylase

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Primary structure and properties of an inactive mutant aspartate transcarbamoylase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)86405-0 ◽

1979 ◽

Vol 254 (23) ◽

pp. 11917-11926

Author(s):

K.A. Wall ◽

H.K. Schachman

Keyword(s):

Primary Structure ◽

Aspartate Transcarbamoylase ◽

Structure And Properties

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Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)34177-2 ◽

1982 ◽

Vol 257 (15) ◽

pp. 8648-8654

Author(s):

D L Burns ◽

H K Schachman

Keyword(s):

Aspartate Transcarbamoylase ◽

Polypeptide Chains

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A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85978-1 ◽

1980 ◽

Vol 255 (5) ◽

pp. 1971-1977

Author(s):

M.A. Bothwell ◽

H.K. Schachman

Keyword(s):

Aspartate Transcarbamoylase ◽

Regulatory Subunits

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Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)35749-6 ◽

1986 ◽

Vol 261 (7) ◽

pp. 3079-3084

Author(s):

R S Lahue ◽

H K Schachman

Keyword(s):

Ligand Binding ◽

Conformational Changes ◽

Active Sites ◽

Aspartate Transcarbamoylase ◽

Polypeptide Chains

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