Relevant bibliographies by topics / SAICAR Synthetase

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Academic literature on the topic 'SAICAR Synthetase'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "SAICAR Synthetase"

1

Škerlová, Jana, Judith Unterlass, Mona Göttmann, et al. "Crystal structures of human PAICS reveal substrate and product binding of an emerging cancer target." Journal of Biological Chemistry 295, no. 33 (2020): 11656–68. http://dx.doi.org/10.1074/jbc.ra120.013695.

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The bifunctional human enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) catalyzes two essential steps in the de novo purine biosynthesis pathway. PAICS is overexpressed in many cancers and could be a promising target for the development of cancer therapeutics. Here, using gene knockdowns and clonogenic survival and cell viability assays, we demonstrate that PAICS is required for growth and survival of prostate cancer cells. PAICS catalyzes the carboxylation of aminoimidazole ribonucleotide (AIR) and the subsequent conversion
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2

Ginder, Nathaniel D., Daniel J. Binkowski, Xiaoming Chen, Jay C. Nix, Herbert J. Fromm, and Richard B. Honzatko. "Entrapment of Phosphoryl Intermediates by SAICAR Synthetase." FASEB Journal 22, S2 (2008): 233. http://dx.doi.org/10.1096/fasebj.22.2_supplement.233.

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3

Wolf, Nina M., Celerino Abad-Zapatero, Michael E. Johnson, and Leslie W. M. Fung. "Structures of SAICAR synthetase (PurC) fromStreptococcus pneumoniaewith ADP, Mg2+, AIR and Asp." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (2014): 841–50. http://dx.doi.org/10.1107/s139900471303366x.

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Streptococcus pneumoniaeis a multidrug-resistant pathogen that is a target of considerable interest for antibacterial drug development. One strategy for drug discovery is to inhibit an essential metabolic enzyme. The seventh step of thede novopurine-biosynthesis pathway converts carboxyaminoimidazoleribonucleotide (CAIR) and L-aspartic acid (Asp) to 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide (SAICAR) in the presence of adenosine 5′-triphosphate (ATP) using the enzyme PurC. PurC has been shown to be conditionally essential for bacterial replication. Two crystal structures of th
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4

Manjunath, Kavyashree, Shankar Prasad Kanaujia, Surekha Kanagaraj, Jeyaraman Jeyakanthan, and Kanagaraj Sekar. "Structure of SAICAR synthetase from Pyrococcus horikoshii OT3: Insights into thermal stability." International Journal of Biological Macromolecules 53 (February 2013): 7–19. http://dx.doi.org/10.1016/j.ijbiomac.2012.10.028.

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5

Wolf, Nina M., Celerino Abad-Zapatero, Michael E. Johnson, and Leslie W. M. Fung. "Structures of SAICAR synthetase (PurC) fromStreptococcus pneumoniaewith ADP, Mg2+, AIR and Asp. Corrigendum." Acta Crystallographica Section D Biological Crystallography 70, no. 11 (2014): 3087. http://dx.doi.org/10.1107/s1399004714022597.

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6

Manjunath, Kavyashree, and Kanagaraj Sekar. "Molecular Dynamics Perspective on the Protein Thermal Stability: A Case Study Using SAICAR Synthetase." Journal of Chemical Information and Modeling 53, no. 9 (2013): 2448–61. http://dx.doi.org/10.1021/ci400306m.

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7

Manjunath, Kavyashree, Jeyaraman Jeyakanthan, and Kanagaraj Sekar. "Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study." Journal of Structural Biology 191, no. 1 (2015): 22–31. http://dx.doi.org/10.1016/j.jsb.2015.06.006.

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8

Ren, Daan, Mark W. Ruszczycky, Yeonjin Ko, et al. "Characterization of the coformycin biosynthetic gene cluster in Streptomyces kaniharaensis." Proceedings of the National Academy of Sciences 117, no. 19 (2020): 10265–70. http://dx.doi.org/10.1073/pnas.2000111117.

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Coformycin and pentostatin are structurally related N-nucleoside inhibitors of adenosine deaminase characterized by an unusual 1,3-diazepine nucleobase. Herein, the cof gene cluster responsible for coformycin biosynthesis is identified. Reconstitution of the coformycin biosynthetic pathway in vitro demonstrates that it overlaps significantly with the early stages of l-histidine biosynthesis. Committed entry into the coformycin pathway takes place via conversion of a shared branch point intermediate to 8-ketocoformycin-5′-monophosphate catalyzed by CofB, which is a homolog of succinylaminoimida
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9

Charoensutthivarakul, Sitthivut, Sherine E. Thomas, Amy Curran, et al. "Development of Inhibitors of SAICAR Synthetase (PurC) from Mycobacterium abscessus Using a Fragment-Based Approach." ACS Infectious Diseases 8, no. 2 (2022): 296–309. http://dx.doi.org/10.1021/acsinfecdis.1c00432.

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10

Manjunath, Kavyashree, Jeyaraman Jeyakanthan, Noriko Nakagawa, et al. "Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of the putative SAICAR synthetase (PH0239) fromPyrococcus horikoshiiOT3." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 2 (2010): 180–83. http://dx.doi.org/10.1107/s1744309109052026.

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Dissertations / Theses on the topic "SAICAR Synthetase"

1

Ginder, Nathaniel Daum. "The structure and mechanism of SAICAR synthetase." [Ames, Iowa : Iowa State University], 2008.

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2

Binkowski, Daniel Joseph. "Kinetic studies of Escherichia coli and human SAICAR synthetase." [Ames, Iowa : Iowa State University], 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3383365.

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3

O'Donnell, Allyson Faye. "Molecular and genetic characterization of AIR carboxylase-SAICAR synthetase in Drosophila melanogaster." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/MQ38399.pdf.

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4

Gao, Xin. "Cloning, expression, and characterization of a recombinant bifunctional protein -- porcine AIR carboxylase and SAICAR synthetase." [Ames, Iowa : Iowa State University], 2006.

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5

Manjunath, Kavyashree. "Structure and Dynamics Studies on SAICAR Synthetase from Pyrococcus horikoshii OT3." Thesis, 2015. http://etd.iisc.ac.in/handle/2005/4181.

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Understanding the structural details of a biological macromolecule is highly essential for a clear interpretation of its functional roles. Structural biology evolved over a period of time has been able to explain various cellular processes which has consequently lead to the discovery of several effective drugs. X-ray crystallography is one of the powerful tools in structural biology, contributing to ∼88% of the three-dimensional structures deposited in the Protein Data Bank (PDB). A single experiment can however provide only one of the numerous conformational states a macromolecule can exhibit
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Journal articles
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