Key reaction components affect the kinetics and performance robustness of cell-free protein synthesis reactions

Autor: Alice M. Banks, Colette J. Whitfield, Steven R. Brown, David A. Fulton, Sarah A. Goodchild, Christopher Grant, John Love, Dennis W. Lendrem, Jonathan E. Fieldsend, Thomas P. Howard

Publikováno v: Computational and Structural Biotechnology Journal, Vol 20, Iss, Pp 218-229 (2022)
Computational and Structural Biotechnology Journal

Graphical abstract
Highlights • Novel cell-free protein synthesis reaction buffer improves performance by 400%. • Enhanced performance is maintained across the synthesis of different proteins. • Protein synthesis performance is robust acro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75d8a1b131f6dc02f2654a6fd7aef7a7
http://www.sciencedirect.com/science/article/pii/S2001037021005213

Determination of Pyruvate Metabolic Fates Modulates Head and Neck Tumorigenesis

Autor: Hsin Ming Chen, Jeng Fan Lo, Ching Wen Chang, Yi Fen Chen, Tz Yu Kuo, Chung Ji Liu, Hao Yuan Chia, Chia Yi Chou, Pei Chun Huang, Tsai Ying Chen, Wan Chun Li, Lu Te Chuang, Yi Ta Hsieh, Jian Min Huang

Publikováno v: Neoplasia: An International Journal for Oncology Research, Vol 21, Iss 7, Pp 641-652 (2019)
Neoplasia (New York, N.Y.)

Even with increasing evidence for roles of glycolytic enzymes in controlling cancerous characteristics, the best target of candidate metabolic enzymes for lessening malignancy remains under debate. Pyruvate is a main glycolytic metabolite that could

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92754b6cd8bfc62335acf4065f363f43
https://doi.org/10.1016/j.neo.2019.04.007

Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity

Autor: Thomas Hicks, Adrián Velázquez-Campoy, Jesús Angulo, Alexis J. Lawton, Pedro Latorre-Muro, John M. Denu, Cristina Hernández-Ruiz, Josue Baeza, Ignacio Delso, José Alberto Carrodeguas, Ramon Hurtado-Guerrero

Publikováno v: Latorre-Muro, P, Baeza, J, Hurtado-Guerrero, R, Hicks, T, Delso, I, Hernández-Ruiz, C, Velázquez-Campoy, A, Lawton, A J, Angulo, J, Denu, J M & Carrodeguas, J A 2021, ' Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity ', Journal of Biological Chemistry, vol. 296, 100205 . https://doi.org/10.1074/jbc.RA120.015103
Digital.CSIC. Repositorio Institucional del CSIC
instname
idUS: Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)
idUS. Depósito de Investigación de la Universidad de Sevilla
The Journal of Biological Chemistry

Acetylation is known to regulate the activity of cytosolic phosphoenolpyruvate carboxykinase (PCK1), a key enzyme in gluconeogenesis, by promoting the reverse reaction of the enzyme (converting phosphoenolpyruvate to oxaloacetate). It is also known t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e83e207f9e31506752cd94b38dcddcdf
http://hdl.handle.net/10261/261527

The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr

Autor: Jun Zhu, Manuela Roggiani, Hui Shi, Mark Goulian, Jane E. Schulte

Publikováno v: The Journal of Biological Chemistry

Histidine phosphorylation is a posttranslational modification that alters protein function and also serves as an intermediate of phosphoryl transfer. Although phosphohistidine is relatively unstable, enzymatic dephosphorylation of this residue is app

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::013d66e3bd5ce2bee10319209ce184cf
https://doi.org/10.1074/jbc.ra120.015121

Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes

Autor: Héctor, Acosta, Richard, Burchmore, Christina, Naula, Melisa, Gualdrón-López, Ender, Quintero-Troconis, Ana J, Cáceres, Paul A M, Michels, Juan Luis, Concepción, Wilfredo, Quiñones

Publikováno v: Molecular and Biochemical Parasitology

Graphical abstract
Highlights • New metabolic routes and membrane proteins were identified in the organelles. • Exponential and stationary growth-phase cells vary little in glycosomal proteins. • A variety of proteins bearing a typical PTS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0f4916d5902a8e2f6bc792a94e5964a9
https://pubmed.ncbi.nlm.nih.gov/30831156