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Journal articles on the topic 'SAICAR Synthetase'

Author: Grafiati

Published: 6 September 2023

Last updated: 19 July 2025

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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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11

Bazurto, Jannell V., Nicholas J. Heitman, and Diana M. Downs. "Aminoimidazole Carboxamide Ribotide Exerts Opposing Effects on Thiamine Synthesis in Salmonella enterica." Journal of Bacteriology 197, no. 17 (2015): 2821–30. http://dx.doi.org/10.1128/jb.00282-15.

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ABSTRACTInSalmonella enterica, the thiamine biosynthetic intermediate 5-aminoimidazole ribotide (AIR) can be synthesizedde novoindependently of the early purine biosynthetic reactions. This secondary route to AIR synthesis is dependent on (i) 5-amino-4-imidazolecarboxamide ribotide (AICAR) accumulation, (ii) a functional phosphoribosylaminoimidazole-succinocarboxamide (SAICAR) synthetase (PurC; EC 6.3.2.6), and (iii) methionine and lysine in the growth medium. Studies presented here show that AICAR is a direct precursor to AIRin vivo. PurC-dependent conversion of AICAR to AIR was recreatedin v

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12

Thomas, Sherine E., Patrick Collins, Rory Hennell James, et al. "Structure-guided fragment-based drug discovery at the synchrotron: screening binding sites and correlations with hotspot mapping." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 377, no. 2147 (2019): 20180422. http://dx.doi.org/10.1098/rsta.2018.0422.

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Structure-guided drug discovery emerged in the 1970s and 1980s, stimulated by the three-dimensional structures of protein targets that became available, mainly through X-ray crystal structure analysis, assisted by the development of synchrotron radiation sources. Structures of known drugs or inhibitors were used to guide the development of leads. The growth of high-throughput screening during the late 1980s and the early 1990s in the pharmaceutical industry of chemical libraries of hundreds of thousands of compounds of molecular weight of approximately 500 Da was impressive but still explored

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13

O'Donnell, Allyson F., Stanley Tiong, David Nash, and Denise V. Clark. "The Drosophila melanogaster ade5 Gene Encodes a Bifunctional Enzyme for Two Steps in the de novo Purine Synthesis Pathway." Genetics 154, no. 3 (2000): 1239–53. http://dx.doi.org/10.1093/genetics/154.3.1239.

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Abstract Steps 6 and 7 of de novo purine synthesis are performed by 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase (SAICARs), respectively. In vertebrates, a single gene encodes AIRc-SAICARs with domains homologous to Escherichia coli PurE and PurC. We have isolated an AIRc-SAICARs cDNA from Drosophila melanogaster via functional complementation with an E. coli purC purine auxotroph. This cDNA encodes AIRc yet is unable to complement an E. coli purE mutant, suggesting functional differences between Drosophila and

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14

Li, Hui, Benshang Li, Fan Yang, et al. "De Novo Purine Biosynthesis in Drug Resistance and Tumor Relapse of Childhood ALL." Blood 126, no. 23 (2015): 2627. http://dx.doi.org/10.1182/blood.v126.23.2627.2627.

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Abstract Background: Relapse is the leading cause of mortality in children with acute lymphoblastic leukemia (ALL). Studies have shown that most ALL cases are polyclonal at diagnosis and that genetic changes in individual subclones influence sensitity to therapy and subsequent clonal evolution during therapy; but the molecular details remain to be worked out. Among different pathways enriched for mutations at relapse, purine metabolism is particularly interesting for two reasons: first, thiopurines are widely used in the ALL combination chemotherapy regimens, and are prodrugs that are converte

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15

Pelet, Anna, Vaclava Skopova, Ulrike Steuerwald, et al. "PAICS deficiency, a new defect of de novo purine synthesis resulting in multiple congenital anomalies and fatal outcome." Human Molecular Genetics 28, no. 22 (2019): 3805–14. http://dx.doi.org/10.1093/hmg/ddz237.

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Abstract We report for the first time an autosomal recessive inborn error of de novo purine synthesis (DNPS)—PAICS deficiency. We investigated two siblings from the Faroe Islands born with multiple malformations resulting in early neonatal death. Genetic analysis of affected individuals revealed a homozygous missense mutation in PAICS (c.158A&gt;G; p.Lys53Arg) that affects the structure of the catalytic site of the bifunctional enzyme phosphoribosylaminoimidazole carboxylase (AIRC, EC 4.1.1.21)/phosphoribosylaminoimidazole succinocarboxamide synthetase (SAICARS, EC 6.3.2.6) (PAICS). The mu

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16

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, January 17, 2022. https://doi.org/10.5281/zenodo.6594009.

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This is the accepted manuscript version of the work published in its final form as Charoensutthivarakul, S., Thomas, S. E., Curran, A., Brown, K. P., Belardinelli, J. M., Whitehouse, A. J., Acebrón-García-de-Eulate, M., Sangan, J., Gramani, S. G., Jackson, M., Mendes, V., Floto, R. A., Blundell, T. L., Coyne, A. G., & Abell, C. (2022). Development of Inhibitors of SAICAR Synthetase (PurC) from <i>Mycobacterium abscessus</i> Using a Fragment-Based Approach. <em>ACS Infectious Diseases</em>, <em>8</em>(2), 296-309. https://doi.org/10.1021/acsinfecdis.1c004

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