21214-07-3Relevant academic research and scientific papers
Identification and characterization of guanosine 5′-monophosphate reductase of Trypanosoma congolense as a drug target
Sarwono, Albertus Eka Yudistira,Suganuma, Keisuke,Mitsuhashi, Shinya,Okada, Tadashi,Musinguzi, Simon Peter,Shigetomi, Kengo,Inoue, Noboru,Ubukata, Makoto
, p. 537 - 544 (2017/07/10)
Trypanosoma congolense is one of the most prevalent pathogens which causes trypanosomosis in African animals, resulting in a significant economic loss. In its life cycle, T. congolense is incapable of synthesizing purine nucleotides via a de novo pathway, and thus relies on a salvage pathway to survive. In this study, we identified a gene from T. congolense, TcIL3000_5_1940, as a guanosine 5′-monophosphate reductase (GMPR), an enzyme that modulates the concentration of intracellular guanosine in the pathogen. The recombinant protein was expressed in Escherichia coli, and the gene product was enzymatically confirmed as a unique GMPR, designated as rTcGMPR. This enzyme was constitutively expressed in glycosomes at all of the parasite's developmental stages similar to other purine nucleotide metabolic enzymes. Mycophenolic acid (MPA) was found to inhibit rTcGMPR activity. Hence, it is a potential lead compound for the design of trypanocidal agents, specifically GMPR inhibitor.
Enzymatic production of 5′-inosinic acid by a newly synthesised acid phosphatase/phosphotransferase
Liu, Zhi-Qiang,Zhang, Ling,Sun, Li-Hui,Li, Xiao-Jun,Wan, Nan-Wei,Zheng, Yu-Guo
experimental part, p. 948 - 956 (2012/08/14)
5′-Nucleotides including 5′-inosinic acid have characteristic taste and important application in various foods as flavour potentiators. The selective nucleoside acid phosphatase/phosphotransferase (AP/PTase) can catalyse the synthesis of 5′-nucleotides by transfer of phosphate groups. In this study, a 747-bp gene encoding AP/PTase from Escherichia blattae was synthesised. After expression, the recombinant AP/PTase was purified using nickel-NTA. The optimal temperature and pH of this enzyme were 30°C and 5.0, respectively. The activity was partially inhibited by metal ions such as Hg2+, Ag+ and Cu2+, but not by chelating reagents such as EDTA. The values of Km and Vmax for inosine were 40 mM and 3.5 U/mg, respectively. Using this purified enzyme, 16.83 mM of 5′-IMP was synthesised from 37 mM of inosine and the molar yield reached 45.5%. Homology modelling and docking simulation were discussed.
