The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase

被引:0
|
作者
Matthew W Vetting
Subray S Hegde
John S Blanchard
机构
[1] Albert Einstein College of Medicine,Department of Biochemistry
来源
Nature Chemical Biology | 2010年 / 6卷
关键词
D O I
暂无
中图分类号
学科分类号
摘要
Some cyclodipeptides are unusual in that their cyclic scaffold is created from activated, amino-acid–loaded tRNA substrates. Structural and biochemical evidence now demonstrates that the enzymes that perform this reaction are homologous to tRNA synthetases and use a covalently bound intermediate.[graphic not available: see fulltext]
引用
收藏
页码:797 / 799
页数:2
相关论文
共 50 条
  • [41] Mutational analysis of the (p)ppGpp synthetase activity of the Rel enzyme of Mycobacterium tuberculosis
    Satyabrata Bag
    Bhabatosh Das
    Shreya Dasgupta
    Rupak K. Bhadra
    Archives of Microbiology, 2014, 196 : 575 - 588
  • [42] RESTORATION OF MYCOLATE SYNTHETASE-ACTIVITY IN MYCOBACTERIUM-TUBERCULOSIS EXPOSED TO ISONIAZID
    TAKAYAMA, K
    ARMSTRONG, EL
    DAVID, HL
    AMERICAN REVIEW OF RESPIRATORY DISEASE, 1974, 110 (01): : 43 - 48
  • [43] The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+ synthetase
    Cantoni, R
    Branzoni, M
    Labò, M
    Rizzi, M
    Riccardi, G
    JOURNAL OF BACTERIOLOGY, 1998, 180 (12) : 3218 - 3221
  • [44] Heterologous expression, purification, and enzymatic activity of Mycobacterium tuberculosis NAD+ synthetase
    Bellinzoni, M
    De Rossi, E
    Branzoni, M
    Milano, A
    Peverali, FA
    Rizzi, M
    Riccardi, G
    PROTEIN EXPRESSION AND PURIFICATION, 2002, 25 (03) : 547 - 557
  • [45] Virtual screening to identify novel potential inhibitors for Glutamine synthetase of Mycobacterium tuberculosis
    Kumari, Madhulata
    Subbarao, Naidu
    JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2020, 38 (17): : 5062 - 5080
  • [46] Mutational analysis of the (p)ppGpp synthetase activity of the Rel enzyme of Mycobacterium tuberculosis
    Bag, Satyabrata
    Das, Bhabatosh
    Dasgupta, Shreya
    Bhadra, Rupak K.
    ARCHIVES OF MICROBIOLOGY, 2014, 196 (08) : 575 - 588
  • [47] Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis
    Grave, Kristine
    Bennett, Matthew D.
    Hogbom, Martin
    COMMUNICATIONS BIOLOGY, 2019, 2 (1)
  • [48] Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis
    Kristīne Grāve
    Matthew D. Bennett
    Martin Högbom
    Communications Biology, 2
  • [49] Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    Tracy A. Young
    Benedicte Delagoutte
    James A. Endrizzi
    Arnold M. Falick
    Tom Alber
    Nature Structural & Molecular Biology, 2003, 10 : 168 - 174
  • [50] The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism
    Gupta, Arvind Kumar
    Behera, Debashree
    Gopal, Balasubramanian
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2018, 74 : 803 - 809