A conservative distribution of tridomain NDP-heptose synthetases in actinobacteria.

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Tytuł:: A conservative distribution of tridomain NDP-heptose synthetases in actinobacteria.
Autorzy:: Tang Y; State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. .
Tang W; State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Wang M; State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhang Z; State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.
Chen Y; State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. .; University of Chinese Academy of Sciences, Beijing, 100049, China. .
Źródło:: Science China. Life sciences [Sci China Life Sci] 2022 May; Vol. 65 (5), pp. 1014-1023. Date of Electronic Publication: 2021 Oct 08.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Original Publication: Beijing : Science China Press, co-published with Springer
MeSH Terms:: Actinobacteria*/genetics
Actinobacteria*/metabolism
Heptoses/chemistry ; Heptoses/metabolism ; Ligases
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Contributed Indexing:: Keywords: Gram-positive bacterium; NDP-heptose biosynthesis; tridomain NDP-heptose synthetase; widespread distribution
Substance Nomenclature:: 0 (Heptoses)
EC 6.- (Ligases)
Entry Date(s):: Date Created: 20211011 Date Completed: 20220512 Latest Revision: 20220716
Update Code:: 20240104
PubMed Central ID:: PMC8502628
DOI:: 10.1007/s11427-021-2000-2
PMID:: 34632535
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Heptoses are important structural components of Gram-negative bacterium cell wall and participate in bacterial colonization, infection, and immune recognition. Current knowledge of NDP-heptose originating from D-sedoheptulose 7-phosphate in Grampositive bacterium remains limited. Here, in silico analysis suggested that the special tridomain NDP-heptose synthetases with isomerase, kinase, and nucleotidyltransferase activities are conservatively distributed in Actinobacteria class of Gram-positive bacterium. Enzymatical characterization of the tridomain proteins from different strains showed that they are involved in ADP-D-glycero-β-D-manno-heptose biosynthesis despite the unexpected discovery of kinase activities deficient in some proteins. The presence of three types of NDP-heptose synthetases in Gram-positive bacterium suggests that it is also a rich source of heptoses and the heptose moieties may play important roles in vivo. Our work updates the understanding of NDP-heptose biosynthesis in Gram-positive bacterium and lays a solid foundation for further physiological function explorations.
(© 2021. Science China Press and Springer-Verlag GmbH Germany, part of Springer Nature.)

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