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27th International Conference on Arginines and Pyrimidines & 2nd International Conference on Amino Acids Nucleotides

A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 8135

Special Issue Editors


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Guest Editor
Leslie Dan Faculty of Pharmacy, University of Toronto, and Krembil Research Institute, University Health Network, Toronto, ON, Canada
Interests: drug discovery; enzyme inhibitors; cannabinoids; psychoactive molecules; multiple sclerosis; inflammatory disorders; mental health
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Guest Editor
The George Washington University School of Medicine and Health, Washington, DC, USA
Interests: molecular biology; cell biology; biochemistry; genomics; bioinformatics; molecular basis of genetic diseases

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Guest Editor
1. Department of Biochemistry, University of Toronto, Toronto, ON, Canada
2. Campbell Family Cancer Research Institute, University Health Network, Toronto, ON, Canada
Interests: structural biology; enzyme mechanisms

Special Issue Information

Dear Colleagues,

ICAP/ICAN 2022 will take place at Chestnut Residence of the University of Toronto in the heart of downtown Toronto, Ontario, Canada on June 28–30th, 2022. This is a biennial conference first organized 55 years ago; and the joint ICAP/ICAN conference has grown to encompass and advance knowledge in amino acids, and nucleic acids as they relate to biological processes, health and disease. The goal of the joint conference is to facilitate interaction and collaboration among attendees from Europe, Asia and the Americas. Participants of the conference, as well as all researchers working in the field are cordially invited to contribute original research papers or reviews to this Special Issue in commemoration of this conference.

Prof. Dr. Lakshmi Kotra
Dr. Ljubica Caldovic
Prof. Dr. Emil F. Pai
Guest Editors

Manuscript Submission Information

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Keywords

  • arginine
  • pyrimidine
  • amino acids
  • nucleotides
  • nucleic acids
  • metabolic enzymes

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Published Papers (3 papers)

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Research

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19 pages, 3943 KiB  
Article
Nucleotide Imbalance, Provoked by Downregulation of Aspartate Transcarbamoylase Impairs Cold Acclimation in Arabidopsis
by Leo Bellin, Diana Laura Garza Amaya, Vanessa Scherer, Tobias Pruß, Annalisa John, Andreas Richter and Torsten Möhlmann
Molecules 2023, 28(4), 1585; https://doi.org/10.3390/molecules28041585 - 7 Feb 2023
Cited by 1 | Viewed by 2053
Abstract
Aspartate transcarbamoylase (ATC) catalyzes the first committed step in pyrimidine de novo synthesis. As shown before, mutants with 80% reduced transcript and protein levels exhibit reduced levels of pyrimidine metabolites and thus nucleotide limitation and imbalance. Consequently, reduced photosynthetic capacity and [...] Read more.
Aspartate transcarbamoylase (ATC) catalyzes the first committed step in pyrimidine de novo synthesis. As shown before, mutants with 80% reduced transcript and protein levels exhibit reduced levels of pyrimidine metabolites and thus nucleotide limitation and imbalance. Consequently, reduced photosynthetic capacity and growth, accompanied by massive transcriptional changes, were observed. Here, we show that nucleotide de novo synthesis was upregulated during cold acclimation of Arabidopsis thaliana (ecotype Columbia, Col-0) plants, but ATC knockdown mutants failed to acclimate to this condition as they did not accumulate neutral sugars and anthocyanins. A global transcriptome analysis revealed that most of the transcriptional changes observed in Col-0 plants upon cold exposure were also evident in ATC knockdown plants. However, several responses observed in cold-treated Col-0 plants could already be detected in knockdown plants when grown under standard conditions, suggesting that these mutants exhibited typical cold responses without prior cold stimulation. We believe that nucleotide signaling is involved in “cold-like priming” and “cold acclimation” in general. The observed transcript levels of genes involved in central carbon metabolism and respiration were an exception to these findings. These were upregulated in the cold but downregulated in warm-grown ATC mutants. Full article
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13 pages, 2130 KiB  
Article
A Tailored Strategy to Crosslink the Aspartate Transcarbamoylase Domain of the Multienzymatic Protein CAD
by Francisco del Caño-Ochoa, Antonio Rubio-del-Campo and Santiago Ramón-Maiques
Molecules 2023, 28(2), 660; https://doi.org/10.3390/molecules28020660 - 9 Jan 2023
Viewed by 2106
Abstract
CAD is a 1.5 MDa hexameric protein with four enzymatic domains responsible for initiating de novo biosynthesis of pyrimidines nucleotides: glutaminase, carbamoyl phosphate synthetase, aspartate transcarbamoylase (ATC), and dihydroorotase. Despite its central metabolic role and implication in cancer and other diseases, our understanding [...] Read more.
CAD is a 1.5 MDa hexameric protein with four enzymatic domains responsible for initiating de novo biosynthesis of pyrimidines nucleotides: glutaminase, carbamoyl phosphate synthetase, aspartate transcarbamoylase (ATC), and dihydroorotase. Despite its central metabolic role and implication in cancer and other diseases, our understanding of CAD is poor, and structural characterization has been frustrated by its large size and sensitivity to proteolytic cleavage. Recently, we succeeded in isolating intact CAD-like particles from the fungus Chaetomium thermophilum with high yield and purity, but their study by cryo-electron microscopy is hampered by the dissociation of the complex during sample grid preparation. Here we devised a specific crosslinking strategy to enhance the stability of this mega-enzyme. Based on the structure of the isolated C. thermophilum ATC domain, we inserted by site-directed mutagenesis two cysteines at specific locations that favored the formation of disulfide bridges and covalent oligomers. We further proved that this covalent linkage increases the stability of the ATC domain without damaging the structure or enzymatic activity. Thus, we propose that this cysteine crosslinking is a suitable strategy to strengthen the contacts between subunits in the CAD particle and facilitate its structural characterization. Full article
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Review

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14 pages, 1978 KiB  
Review
Bench-to-Bedside Studies of Arginine Deprivation in Cancer
by George C. Field, Iuliia Pavlyk and Peter W. Szlosarek
Molecules 2023, 28(5), 2150; https://doi.org/10.3390/molecules28052150 - 24 Feb 2023
Cited by 12 | Viewed by 2786
Abstract
Arginine is a semi-essential amino acid which becomes wholly essential in many cancers commonly due to the functional loss of Argininosuccinate Synthetase 1 (ASS1). As arginine is vital for a plethora of cellular processes, its deprivation provides a rationale strategy for combatting arginine-dependent [...] Read more.
Arginine is a semi-essential amino acid which becomes wholly essential in many cancers commonly due to the functional loss of Argininosuccinate Synthetase 1 (ASS1). As arginine is vital for a plethora of cellular processes, its deprivation provides a rationale strategy for combatting arginine-dependent cancers. Here we have focused on pegylated arginine deiminase (ADI-PEG20, pegargiminase)–mediated arginine deprivation therapy from preclinical through to clinical investigation, from monotherapy to combinations with other anticancer therapeutics. The translation of ADI-PEG20 from the first in vitro studies to the first positive phase 3 trial of arginine depletion in cancer is highlighted. Finally, this review discusses how the identification of biomarkers that may denote enhanced sensitivity to ADI-PEG20 beyond ASS1 may be realized in future clinical practice, thus personalising arginine deprivation therapy for patients with cancer. Full article
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