One-pot enzymatic synthesis of deoxy-thymidine-diphosphate (TDP)-2-deoxy-α-d-glucose using phosphomannomutase

Autor:	Yung-Hum Yang, Kwangkyung Liou, Jae Kyung Sohng, Tek-Hyung Lee, Kwangwon Lee, Hee-Chan Lee, Byung-Gee Kim, Young Bok Abraham Kang, Dongwon Yoo, Sung-Hee Park, Dae-Hee Kim
Rok vydání:	2010
Předmět:	Acetate kinase Thymidine diphosphate biology Stereochemistry Process Chemistry and Technology Bioengineering Isomerase Biochemistry Catalysis chemistry.chemical_compound chemistry D-Glucose Glycosyltransferase biology.protein Phosphoglucomutase Specific activity Phosphomannomutase
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 62:282-287
ISSN:	1381-1177
DOI:	10.1016/j.molcatb.2009.11.008
Popis:	Production of deoxy-thymidine-diphosphate (TDP)-sugars as substrates of glycosyltransferases, has been one of main hurdles for combinatorial antibiotic biosynthesis, which combines sugar moiety with aglycon of various antibiotics. Here, we report the one-pot enzymatic synthesis of TDP-2-deoxy-glucose employing high efficient TMP kinase (TMK; E.C. 2.7.2.12), acetate kinase (ACK; E.C. 2.7.1.21), and TDP-glucose synthase (TGS; E.C. 2.7.7.24) with phosphomannomutase (PMM; E.C. 5.4.2.8). In this study, replacing phosphoglucomutase (PGM; E.C. 5.4.2) by PMM from Escherichia coli gave four times higher specific activity on 2-deoxy-6-phosphate glucose, suggesting that the activity on 2-deoxy-glucose-6-phosphate was mainly affected by PMM activity, not PGM activity. Using an in vitro system starting from TMP and 2-deoxy-glucose-6-phosphate glucose, TDP-2-deoxy-glucose (63% yield) was successfully synthesized. Considering low productivity of NDP-sugars from cheap starting materials, this paper showed how production of NDP-sugars could be enhanced by controlling mutase activity.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8219831ddc07e67d55cae0722b27574c https://doi.org/10.1016/j.molcatb.2009.11.008 Zobrazit plný text záznamu Full Text from ScienceDirect