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Annemie Jacobs

Researcher at Vrije Universiteit Brussel

Publications -  5
Citations -  126

Annemie Jacobs is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Allosteric regulation & Aspartate carbamoyltransferase. The author has an hindex of 5, co-authored 5 publications receiving 126 citations. Previous affiliations of Annemie Jacobs include VU University Amsterdam.

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Journal ArticleDOI

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.

TL;DR: The result shows that the hydrophobic interface between the two domains of the regulatory chain plays an important role in the discrimination between the regulatory signals promoted by the two allosteric effectors.
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Positive and negative regulation of CAR1 Expression in Saccharomyces cerevisiae

TL;DR: Fusion tolacZ of several fragments of the 5′ non-coding region showed that induction ofCAR1 by arginine is positively regulated by the products of theARGR genes, and the order of the regulatory regions was confirmed: 5′—nitrogen catabolite repression—activation byArginine—CARGRI-mediated repression—CAR1.
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Intramolecular transmission of the ATP regulatory signal in Escherichia coli aspartate transcarbamylase: specific involvement of a clustered set of amino acid interactions at an interface between regulatory and catalytic subunits.

TL;DR: The identification of a cluster of amino acid interactions at an interface between the regulatory chains and the catalytic chains of the enzyme as another structural feature involved in the transmission of the ATP regulatory signal but not in those of CTP and UTP is described.
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The Activation of Escherichia coli Aspartate Transcarbamylase by ATP: Specific Involvement of Helix H2′ at the Hydrophobic Interface Between the Two Domains of the Regulatory Chains

TL;DR: The properties of the mutants and the results of modelling suggest that a movement of helix H2' is part of the mechanism of activation by ATP, and a model is proposed to account for the transmission of the ATP signal from the regulatory site to the interface between the regulatory and catalytic chains.
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Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI gene encoding a modified regulatory subunit.

TL;DR: The sequence of the mutated pyrI gene is reported and it is shown that, during the generation of this pyrBI-bearing phage, six codons from lambda DNA have been substituted for the eight terminal codons of the wild-type gene.