Modes of modifier action in E. coli aspartate transcarbamylase (Q52902759)

9 May 2018

title

Modes of modifier action in E. coli aspartate transcarbamylase (English)

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https://api.crossref.org/works/10.1016/0003-9861(74)90455-X

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https://api.crossref.org/works/10.1016/0003-9861(74)90455-X

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author name string

F. C. Wedler

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A4604784

11 February 2023

F. J. Gasser

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A4604784

11 February 2023

language of work or name

English

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publication date

1 July 1974

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9 May 2018

full work available at URL

number of pages

10

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based on heuristic

inferred from page(s)

https://api.elsevier.com/content/article/PII:000398617490455X?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/0003-9861(74)90455-X

https://api.elsevier.com/content/article/PII:000398617490455X?httpAccept=text/plain

11 February 2023

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https://api.crossref.org/works/10.1016/0003-9861(74)90455-X

Archives of Biochemistry and Biophysics

11 February 2023

published in

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9 May 2018

volume

163

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9 May 2018

issue

1

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9 May 2018

page(s)

69-78

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9 May 2018

Subunit interactions in aspartate transcarbamylase

cites work

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An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate

11 February 2023

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Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase

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Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase

11 February 2023

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Structure and arrangement of the regulatory subunits in aspartate transcarbamylase

11 February 2023

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Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

11 February 2023

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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate

11 February 2023

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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5'-triphosphate.

11 February 2023

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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analog

11 February 2023

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Studies with aspartate transcarbamylase

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Binding of succinate to aspartate transcarbamylase catalytic subunit. The pH and temperature dependence of nuclear magnetic resonance relaxation times

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Kinetic and binding effects of 1,N 6 -ethenoadenosine triphosphate to aspartate transcarbamylase.

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An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions

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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs

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Model for nucleotide regulation of aspartate transcarbamylase

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Uses and limitations of measurements of rates of isotopic exchange and incorporation in catalyzed reactions

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Mechanisms of enzyme control as probed by equilibrium exchange rates: patterns of modifier effects with a two substrate, two product system

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Ordered substrate binding and evidence for a thermally induced change in mechanism for E. coli aspartate transcarbamylase

11 February 2023

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Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits

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Anomalous pH dependence of Kcat/Km in enzyme reactions. Rate constants for the association of chymotrypsin with substrates

11 February 2023

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Extensions of the Allosteric Model for Haemoglobin

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Enzyme forms produced from aspartate transcarbamoylase by digestion with trypsin

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Identifiers

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9 May 2018

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9 May 2018