(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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1 June 2018

Ley BW

2

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1 June 2018

Kantrowitz ER

3

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1 June 2018

O'Leary MH

4

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1 June 2018

Wedler FC

5

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1 June 2018

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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1 June 2018

issue

26

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1 June 2018

page(s)

15620-15627

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1 June 2018

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

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

Escherichia coli aspartate transcarbamylase: the relation between structure and function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

Multiple isotope effects on enzyme-catalyzed reactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

The contribution of threonine 55 to catalysis in aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

A continuous visible spectrophotometric assay for aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

DECOMPOSITION OF CARBAMYLPHOSPHATE IN AQUEOUS SOLUTIONS

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15620

21 January 2018

Identifiers

DOI

10.1074/JBC.270.26.15620

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1 June 2018

PubMed ID

7797560

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1 June 2018