(Q72191070)

English

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

scientific article published on 01 April 1995

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7730350%20AND%20SRC:MED&resulttype=core&format=json

24 October 2019

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 (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7730350%20AND%20SRC:MED&resulttype=core&format=json

24 October 2019

Escherichia coli

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F C Wedler

1

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24 October 2019

B W Ley

2

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24 October 2019

B H Lee

3

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24 October 2019

M H O'Leary

4

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24 October 2019

E R Kantrowitz

5

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24 October 2019

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1 April 1995

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24 October 2019

Journal of Biological Chemistry

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7730350%20AND%20SRC:MED&resulttype=core&format=json

24 October 2019

270

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24 October 2019

17

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24 October 2019

9725-9733

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24 October 2019

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Escherichia coli aspartate transcarbamylase: the relation between structure and function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

The contribution of threonine 55 to catalysis in aspartate transcarbamoylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Kinetic mechanism of catalytic subunits (c3) of E. coli aspartate transcarbamylase at pH 7.0.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

A continuous visible spectrophotometric assay for aspartate transcarbamylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

DECOMPOSITION OF CARBAMYLPHOSPHATE IN AQUEOUS SOLUTIONS

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Rate-limiting step: a quantitative definition. Application to steady-state enzymic reactions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.9725

21 January 2018

Identifiers

10.1074/JBC.270.17.9725

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7730350%20AND%20SRC:MED&resulttype=core&format=json

24 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7730350%20AND%20SRC:MED&resulttype=core&format=json

24 October 2019

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