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Showing 1–13 of 13 results
Advanced filters: Author: Squire J. Booker Clear advanced filters

  • LipCo biosynthesis in humans depends exclusively on a de novo pathway involving LIPT2, LIAS, and LIPT1. In this work authors present structures of LIAS captured in multiple catalytic states, revealing critical conformational changes associated with the reaction. The structures of the LIAS–Hpro complex define molecular interactions essential for complex formation. These structures enabled the mapping of amino acid changes associated with non-ketotic hyperglycemia.

    • Olga A. Esakova
    • Douglas M. Warui
    • Squire J. Booker
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • Enzymes with identical sequences of amino acids can display varying activities when encoded with mRNA with different properties, but why this is the case has been a mystery. Now, it has been shown that synonymous mutations in mRNA alter the partitioning of proteins into long-lived soluble misfolded states with varying activities.

    • Yang Jiang
    • Syam Sundar Neti
    • Edward P. O’Brien
    Research
    Nature Chemistry
    Volume: 15, P: 308-318

  • The radical S-adenosylmethionine (SAM) enzyme, AbmM, catalyses a replacement of the ring oxygen of a sugar with sulfur. However, how this reaction takes place is unknown. Now, an [Fe4S4] cluster is shown to have a dual role in catalysis. It functions in the reductive cleavage of SAM and is the donor of the appended sulfur atom.

    • Olga A. Esakova
    • Squire J. Booker
    News & Views
    Nature Catalysis
    Volume: 8, P: 758-759

  • The enzyme co-substrate SAM has long been known to have two chemically distinct roles. A study of the CmoA enzyme suggests that SAM has a third trick up its sleeve — it forms species known as ylides. See Letter p.123

    • Bradley J. Landgraf
    • Squire J. Booker
    News & Views
    Nature
    Volume: 498, P: 45-47

  • The radical SAM superfamily of enzymes provides, yet again, fertile ground for the discovery of amazing new biochemical transformations. Strong evidence is now presented for an unprecedented radical fragmentation-recombination of L-tryptophan to a derivative that is incorporated into the complex antibiotic nosiheptide, highlighting the versatility of radical mechanisms for complex biochemical reactions.

    • Arthur J Arcinas
    • Squire J Booker
    News & Views
    Nature Chemical Biology
    Volume: 7, P: 133-134

  • X-ray crystal structures of TokK, a cobalamin- or B12-dependent radical SAM methylase, provide insight into how these enzymes use sequential radical-mediated methylations to assemble the C6 side chain of carbapenem antibiotics.

    • Hayley L. Knox
    • Erica K. Sinner
    • Squire J. Booker
    Research
    Nature
    Volume: 602, P: 343-348

  • Crystal structures of a cobalamin-dependent radical S-adenosylmethionine (SAM) methylase reveal an unexpected mechanism that involves substrate-assisted catalysis whereby the carboxylate group of the co-substrate SAM serves as a general base.

    • Hayley L. Knox
    • Percival Yang-Ting Chen
    • Squire J. Booker
    Research
    Nature Chemical Biology
    Volume: 17, P: 485-491

  • Mitochondrial ferredoxins FDX1 and FDX2 are assigned to specifically donate electrons to steroidogenesis, Fe–S protein biogenesis, heme a formation or lipoylation. The proteins’ functions can be swapped by mutually exchanging short peptide segments.

    • Vinzent Schulz
    • Somsuvro Basu
    • Roland Lill
    Research
    Nature Chemical Biology
    Volume: 19, P: 206-217

  • The radical SAM enzyme Cfr catalyzes methylation of a ribosomal adenosine, causing broad antibiotic resistance. EPR and ENDOR techniques now provide direct evidence for the proposed enzymatic mechanism by detecting a central crosslinked intermediate in which a radical is located on the nucleotide.

    • Tyler L Grove
    • Jovan Livada
    • Alexey Silakov
    Research
    Nature Chemical Biology
    Volume: 9, P: 422-427