skip to main content
Ngôn ngữ:
Giới hạn tìm kiếm: Giới hạn tìm kiếm: Dạng tài nguyên Hiển thị kết quả với: Hiển thị kết quả với: Chỉ mục

Deletion of a dehydratase important for intracellular growth and cording renders rough Mycobacterium abscessus avirulent

Halloum, Iman ; Carrere-Kremer, Severine ; Blaise, Mickaël ; Viljoen, Albertus ; Bernut, Audrey ; Le Moigne, Vincent ; Vilchèze, Catherine ; Guérardel, Yann ; Lutfalla, Georges ; Herrmann, Jean-Louis ; Jacobs, William ; Kremer, Laurent; Lutfalla, Georges (Editor)

Proceedings of the National Academy of Sciences of the United States of America, 19 July 2016, Vol.113(29), pp.E4228-E4237 [Tạp chí có phản biện]

ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1605477113

Toàn văn sẵn có

Trích dẫn Trích dẫn bởi
  • Nhan đề:
    Deletion of a dehydratase important for intracellular growth and cording renders rough Mycobacterium abscessus avirulent
  • Tác giả: Halloum, Iman ; Carrere-Kremer, Severine ; Blaise, Mickaël ; Viljoen, Albertus ; Bernut, Audrey ; Le Moigne, Vincent ; Vilchèze, Catherine ; Guérardel, Yann ; Lutfalla, Georges ; Herrmann, Jean-Louis ; Jacobs, William ; Kremer, Laurent
  • Lutfalla, Georges (Editor)
  • Chủ đề: Life Sciences ; Immunology ; Life Sciences ; Immunology ; Innate Immunity ; Life Sciences ; Microbiology and Parasitology ; Bacteriology ; Life Sciences ; Microbiology and Parasitology ; Sciences (General)
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States of America, 19 July 2016, Vol.113(29), pp.E4228-E4237
  • Mô tả: Using a large-scale "genomic enzymology" approach, we (i) assigned novel ATP-dependent four-carbon acid sugar kinase functions to members of the DUF1537 protein family (domain of unknown function; Pfam families PF07005 and PF17042) and (ii) discovered novel catabolic pathways for D-threonate, L-threonate, and D-erythronate. The experimentally determined ligand specificities of several solute binding proteins (SBPs) for TRAP (tripartite ATP-independent permease) transporters for four-carbon acids, including D-erythronate and L-erythronate, were used to constrain the substrates for the catabolic pathways that degrade the SBP ligands to intermediates in central carbon metabolism. Sequence similarity networks and genome neighborhood networks were used to identify the enzyme components of the pathways. Conserved genome neighborhoods encoded SBPs as well as permease components of the TRAP transporters, members of the DUF1537 family, and a member of the 4-hydroxy-L-threonine 4-phosphate dehydrogenase (PdxA) oxidative decarboxylase, class II aldolase, or ribulose 1,5-bisphosphate carboxylase/oxygenase, large subunit (RuBisCO) superfamily. Because the characterized substrates of members of the PdxA, class II aldolase, and RuBisCO superfamilies are phosphorylated, we postulated that the members of the DUF1537 family are novel ATP-dependent kinases that participate in catabolic pathways for four-carbon acid sugars. We determined that (i) the DUF1537/PdxA pair participates in a pathway for the conversion of D-threonate to dihydroxyacetone phosphate and C[O.sub.2] and (ii) the DUF1537/class II aldolase pair participates in pathways for the conversion of D-erythronate and L-threonate (epimers at carbon-3) to dihydroxyacetone phosphate and C[O.sub.2]. The physiological importance of these pathways was demonstrated in vivo by phenotypic and genetic analyses. DUF1537 | kinase | four-carbon acid sugars | conserved genome neighborhoods | genomic enzymology
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1605477113

Đang tìm Cơ sở dữ liệu bên ngoài...