Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism. (Q54610153)

1 June 2018

title

Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism. (English)

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1 June 2018

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Lee BH

1

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Ley BW

2

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Kantrowitz ER

3

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O'Leary MH

4

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Wedler FC

5

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language of work or name

English

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publication date

1 June 1995

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1 June 2018

Journal of Biological Chemistry

number of pages

8

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based on heuristic

inferred from page(s)

published in

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1 June 2018

volume

270

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issue

26

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page(s)

15620-15627

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1 June 2018

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

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Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli.

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A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

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Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase.

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Escherichia coli aspartate transcarbamylase: the relation between structure and function

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Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.

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Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.

21 January 2018

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Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure

21 January 2018

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Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor

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Multiple isotope effects on enzyme-catalyzed reactions

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Carbon-13 isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase

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Carbon-13 and nitrogen-15 isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase

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Carbon-13 isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate

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The contribution of threonine 55 to catalysis in aspartate transcarbamoylase

21 January 2018

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Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

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Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.

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Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms

21 January 2018

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Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine

21 January 2018

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L-aspartate association contributes to rate limitation and induction of the T-->R transition in Escherichia coli aspartate transcarbamoylase. Equilibrium exchanges and kinetic isotope effects with a Vmax-enhanced mutant, Asp-236-->Ala

21 January 2018

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A continuous visible spectrophotometric assay for aspartate transcarbamylase

21 January 2018

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DECOMPOSITION OF CARBAMYLPHOSPHATE IN AQUEOUS SOLUTIONS

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.26.15620

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1 June 2018

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1 June 2018