This recombinant Schizosaccharomyces pombe Thymidylate kinase (tmp1) protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Thymidylate kinase (TMPK), encoded by the tmp1 gene, is an essential enzyme regulating DNA biosynthesis in various organisms. TMPK phosphorylates deoxythymidine monophosphate (dTMP) into deoxythymidine diphosphate (dTDP) using ATP as a phosphate donor [1]. It is crucial for DNA replication and repair [2]. TMPK plays a vital role in maintaining the balance of dTTP pool size, which is essential for genetic stability during cell division [3].
In addition to its physiological function, TMPK is required for activating thymidine analogs like AZT and d4T, which are used as anti-HIV prodrugs [4]. Due to its essential role in bacterial DNA biosynthesis, TMPK has been a target for developing antibacterial agents, especially against Mycobacterium tuberculosis, the causative agent of tuberculosis [5][6].
References:
[1] J. Su and R. Sclafani, Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast, Nucleic Acids Research, vol. 19, no. 4, p. 823-827, 1991. https://doi.org/10.1093/nar/19.4.823
[2] C. Hu, M. Yeh, N. Tsao, C. Chen, Q. Gao, C. Changet al., Tumor cells require thymidylate kinase to prevent dutp incorporation during dna repair, Cancer Cell, vol. 22, no. 1, p. 36-50, 2012. https://doi.org/10.1016/j.ccr.2012.04.038
[3] P. Ke, Y. Kuo, C. Hu, & Z. Chang, Control of dttp pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability, Genes & Development, vol. 19, no. 16, p. 1920-1933, 2005. https://doi.org/10.1101/gad.1322905
[4] A. Lavie and M. Konrad, Structural requirements for efficient phosphorylation of nucleotide analogs by human thymidylate kinase, Mini-Reviews in Medicinal Chemistry, vol. 4, no. 4, 2004. https://doi.org/10.2174/1389557043403981
[5] L. Song, R. Merceron, B. Gracia, A. Quintana, M. Risseeuw, F. Hulpiaet al., Structure guided lead generation toward nonchiral m. tuberculosis thymidylate kinase inhibitors, Journal of Medicinal Chemistry, vol. 61, no. 7, p. 2753-2775, 2018. https://doi.org/10.1021/acs.jmedchem.7b01570
[6] S. Kawatkar, T. Keating, N. Olivier, J. Breen, O. Green, S. Guleret al., Antibacterial inhibitors of gram-positive thymidylate kinase: structure–activity relationships and chiral preference of a new hydrophobic binding region, Journal of Medicinal Chemistry, vol. 57, no. 11, p. 4584-4597, 2014. https://doi.org/10.1021/jm500463c
