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Showing 1–11 of 11 results
Advanced filters: Author: Yi-Ling Du Clear advanced filters
  • Despite the existence of many N–N-containing natural metabolites, little is known about the enzymatic mechanisms of N–N bond formation. Now, a catalytically relevant X-ray crystal structure of an N–N-bond-forming enzyme, PipS, is reported and detailed insights into its catalytic mechanism are provided.

    • Melanie A. Higgins
    • Xinjie Shi
    • Katherine S. Ryan
    Research
    Nature Catalysis
    Volume: 8, P: 207-217
  • How nature creates 1,2,3-triazole ring is a relevant question to N-N bond biosynthesis. Here, the authors report the biosynthetic route to the triazole-bearing antimetabolite 8-azaguanine and reveal that this can be assembled through an enzymatic and non-enzymatic cascade, in which nitric oxide is used as a building block.

    • Guiyun Zhao
    • Yuan-Yang Guo
    • Yi-Ling Du
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10
  • Tryptophan hydroxylases have only been known from eukaryotes and are involved in the biosynthesis of serotonin or melatonin. Here, the authors characterize a family of bacterial tryptophan hydroxylases that differ markedly from their eukaryotic counterpart in cofactor and catalytic mechanism.

    • Xinjie Shi
    • Guiyun Zhao
    • Yi-Ling Du
    Research
    Nature Chemical Biology
    Volume: 19, P: 1415-1422
  • Characterization of the heme-dependent enzyme KtzT reveals it to be the elusive enzyme responsible for nitrogen–nitrogen bond formation during the biosynthesis of piperazate, a building block for some nonribosomal peptide natural products.

    • Yi-Ling Du
    • Hai-Yan He
    • Katherine S Ryan
    Research
    Nature Chemical Biology
    Volume: 13, P: 836-838
  • Enzymes involved in the synthesis of nitrogen-nitrogen bond containing molecules have been identified but the processes remain largely unknown. Here, the authors use biochemical characterisation and computer modelling to study the molecular basis of hydrazine bond formation by a family of di-domain enzymes.

    • Guiyun Zhao
    • Wei Peng
    • Yi-Ling Du
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10
  • Azoxy bonds are frequently found in liquid crystals, chemical intermediates, dyes, agrochemicals and pharmaceuticals. Here, the authors investigated azoxy bond formation by the non-heme diiron N-oxygenase AzoC in azoxymycin biosynthesis and show that the nitroso group plays a key part in it.

    • Yuan-Yang Guo
    • Zhen-Hua Li
    • Yong-Quan Li
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9
  • The indolmycin biosynthetic pathway in a marine gram-negative bacterium is distinct from its counterpart in terrestrial gram-positive Streptomyces species, using a Streptomyces shunt product as a substrate for an N-demethylindolmycin synthase.

    • Yi-Ling Du
    • Melanie A. Higgins
    • Katherine S. Ryan
    Research
    Nature Chemical Biology
    Volume: 15, P: 1043-1048
  • Pyridoxal 5-phosphate (PLP) is an essential coenzyme involved in diverse amino acid transformations. The discovery that Ind4 catalyzes the PLP-dependent oxidation of an unactivated carbon of L-arginine, as a part of the indolmycin biosynthetic pathway, expands the scope of reactions facilitated by PLP-dependent enzymes.

    • Yi-Ling Du
    • Rahul Singh
    • Katherine S Ryan
    Research
    Nature Chemical Biology
    Volume: 12, P: 194-199
  • Triacylglycerides are naturally abundant and renewable feedstock, but their chemical transformation is hindered by their stability. Here, under Lewis acid catalysis, the authors report the selective alkyl C–O bond conversion of triglycerides into C–N bonds and even apply this efficient method to PET depolymerization.

    • Hua Liu
    • Yi-Ling Zhu
    • Zhi Li
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10